Information on EC 1.12.7.2 - ferredoxin hydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.12.7.2
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RECOMMENDED NAME
GeneOntology No.
ferredoxin hydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carbon monoxide dehydrogenase complex
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hydrogen production III
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hydrogen production VI
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hydrogen production VIII
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L-glutamate degradation VII (to butanoate)
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superpathway of fermentation (Chlamydomonas reinhardtii)
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hydrogen production
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:ferredoxin oxidoreductase
Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances.
CAS REGISTRY NUMBER
COMMENTARY hide
9080-02-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
strain ATC 19859
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Manually annotated by BRENDA team
Acutodesmus obliquus
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
archaebacterium
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain 137 C(+)
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Manually annotated by BRENDA team
Chlorococcum submarinum
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain MR 505
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Manually annotated by BRENDA team
strain H16, ATCC 17699
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
Desulfovibrio vulgaris Hildenborough ATCC 29579
strain Hildenborough ATCC 29579
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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1031893 A+, 1045916 A+, 1046144 A+, 1048006 A+, 1048052 A+, 1054255 A+, 1075893 A+, 1075901 A+, 1075948 A+, 1075953 A+, 1076004 A+, 1076008 A+, 1076049 A+, 1076068 A+, 1076077 A+, 1076085 A+, 1076099 A+, 1076100 A+, 1076105 A+, 1076111 A+, 1076116 A+, 1076125 A+, 1076128 A+, 1076130 A+, 1076132 A+, 1076137 A+, 1076155 A+, 1076156 A+, 1076157 A+, 1076158 A+, 1076167 A+, 1076171 A+, 1076176 A+, 1076190 A+, 1076201 A+, 1076210 A+, 1076219 A+, 1076222 A+, 1076269 A+, 1076278 A+, 1076294 A+, 1076296 A+, 1076303 A+, 1076306 A+, 1076312 A+, 1076321 A+, 1076332 A+, 1076340 A+, 1076349 A+, 1076351 A+, 1076385 A+, 1076400 A+, 1076426 A+, 1076436 A+, 1076466 A+, 1076473 A+, 1076506 A+, 1076552 A+, 1076585 A+, 1076587 A+, 1076598 A+, 1076599 A+, 1076605 A+, 1076614 A+, 1076622 A+, 1090459 A+, 1090466 A+, 1090471 A+, 1202439 A+, 1237725 A+, 1237919 A+, 1238351 A+, 1238918 A+, 1239377 A+, 1250739 A+, 1250740 A+, 1250836 A+, 1251343 A+, 1251798 A+, 1251945 A+, 1376195 A+, 1425472 A+, 1542252 A+, 1543408 A+, 1546695 A+, 1636934 A+, 1642921 A+, 1643125 A+, 1678862 A+, 1678868 A+, 1679038 A+, 1679228 A+, 1688306 A+, 1704049 A+, 1704073 A+, 1704075 A+, 1704090 A+, 1704130 A+, 1704151 A+, 1704153 A+, 1704185 A+, 1704397 A+, 1704414 A+, 1731760 A+, 1735240 A+, 1746766 A+, 1746861 A+, 1766359 A+, 1766978 A+, 1768340 A+, 1768364 A+, 1807666 A+, 1846640 A+, 1846651 A+, 1846672 A+, 1846695 A+, 1846709 A+, 1846712 A+, 1846715 A+, 1846770 A+, 1846777 A+, 1846797 A+, 1846804 A+, 1846820 A+, 1846826 A+, 1846842 A+, 1846844 A+, 1846845 A+, 1846851 A+, 1846855 A+, 1846857 A+, 1846858 A+, 1846864 A+, 1846876 A+, 1846884 A+, 1846888 A+, 1846891 A+, 1846914 A+, 1846916 A+, 1846923 A+, 1846924 A+, 1846962 A+, 1846968 A+, 1846973 A+, 1846992 A+, 1846995 A+, 1846997 A+, 1847001 A+, 1847009 A+, 1847011 A+, 1847014 A+, 1847016 A+, 1847022 A+, 1847026 A+, 1847035 A+, 1847040 A+, 1847054 A+, 1847060 A+, 1847064 A+, 1847068 A+, 1847072 A+, 1847075 A+, 1847078 A+, 1847079 A+, 1847085 A+, 1847088 A+, 2102747 A+, 2266807 A+, 2283872 A+, 2283891 A+, 2283943 A+, 2283955 A+, 2283956 A+, 2283960 A+, 2283961 A+, 2283962 A+, 2283965 A+, 2283969 A+, 2283970 A+, 2283972 A+, 2283974 A+, 2283975 A+, 2283976 A+, 2283980 A+, 2283988 A+, 2283995 A+, 2283998 A+, 2284019 A+, 2284020 A+, 2284024 A+, 2284034 A+, 2284038 A+, 2399738 A+, 2400393 A+, 2746705 A+, 2751798 A+, 2765564 A+, 2765608 A+, 2879498 A+, 2879533 A+, 2879535 A+, 2879538 A+, 2879542 A+, 2879544 A+, 2879547 A+, 2879554 A+, 2879556 A+, 2879562 A+, 2879583 A+, 2879593 A+, 2879598 A+, 2879604 A+, 2879607 A+, 2879610 A+, 2879611 A+, 2879614 A+, 2879616 A+, 2879643 A+, 2879650 A+, 2879651 A+, 2879652 A+, 2879654 A+, 2879663 A+, 393939 A+, 395086 A+, 395098 A+, 395563 A+, 395565 A+, 395571 A+, 395574 A+, 439632 A+, 439641 A+, 439647 A+, 439652 A+, 439654 A+, 439659 A+, 439660 A+, 439661 A+, 439672 A+, 439674 A+, 439676 A+, 439691 A+, 439703 A+, 441750 A+, 485661 A+, 654261 A+, 654899 A+, 655307 A+, 655396 A+, 655575 A+, 659019 A+, 659110 A+, 659878 A+, 667270 A+, 672279 A+, 672350 A+, 672638 A+, 672729 A+, 673710 A+, 674924 A+, 675360 A+, 675496 A+, 677009 A+, 685627 A+, 701758 A+, 712281 A+, 713401 A+, 713413 A+, 722483 A+, 724456 A+, 725269 A+, 730867 A+, 735729 A+, 737856 A+, 738132 A+, 986326 A+, 1003778 A++, 1048054 A++, 1048070 A++, 1076037 A++, 1076608 A++, 1076644 A++, 1847006 A++, 1847036 A++, 1847081 A++, 2266788 A++, 2283898 A++, 2283916 A++, 2283940 A++, 2284026 A++, 2284029 A++, 2284032 A++, 2879618 A++, 2879629 A++, 726038 A++, 1076575 A++, 1090483 A++, 1846697 A++, 1846714 A++, 2266797 A++, 2283948 A++, 2284030 A++, 2284033 A++, 2284035 A++, 711817 A++, 728673 A++, 1076129 A+++, 1076203 A+++, 1076204 A+++, 1076285 A+++, 1076374 A+++, 1076398 A+++, 1076412 A+++, 1076413 A+++, 1076520 A+++, 1076550 A+++, 1076564 A+++, 395568 A+++, 439675 A+++, 644673 A+++, 1076603 A++++, 1076609 A++++
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
IIT-BT08 (MTCC 5373)
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain LC1, formerly Peptostreptococcus elsdenii
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain Fusaro DSM 804
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Manually annotated by BRENDA team
strain MS, DSM 800
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
rumen bacterium
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain NCIM 1605
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Manually annotated by BRENDA team
Tetraselmis sp. KSN-2002 NCIM 1605
strain NCIM 1605
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(SeO3)2- + H2 + ?
Se + H2O + ?
show the reaction diagram
(TeO3)2- + H2 + ?
Te + H2O + ?
show the reaction diagram
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
show the reaction diagram
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
show the reaction diagram
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58.8% relative activity, purified enzyme
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?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
H2 + 2 oxidized ferredoxin
2 reduced ferredoxin + 2 H+
show the reaction diagram
Q8U0Z8 and Q8U0Z7 and Q8U0Z6
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?
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
show the reaction diagram
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
show the reaction diagram
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wild-type enzyme catalysed the reduction of benzylviologen at fourfold higher rates than the reduction of ferredoxin
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?
H2 + oxidized CAC3527 ferredoxin
H+ + reduced CAC3527 ferredoxin
show the reaction diagram
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mutant CAC3527 ferredoxin displays an almost 8fold lower reduction potential than wild type ferredoxin
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r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
H2 + oxidized ferredoxin
reduced ferredoxin + 2 H+
show the reaction diagram
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?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
H2 + oxidized ferredoxin CAC0587
H+ + reduced ferredoxin CAC0587
show the reaction diagram
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ferredoxin CAC0587 is the standard major ferredoxin
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r
H2 + oxidized flavodoxin CAC0587
H+ + reduced flavodoxin CAC0587
show the reaction diagram
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flavodoxin CAC0587 is the standard major flavodoxin
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r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
S + NADPH
H2S + NADP+
show the reaction diagram
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
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the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
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?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
show the reaction diagram
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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hydrogenase II, 0.83 mol per mol heterotetramer; putative nucleotide-binding site in the gamma subunit
Ferredoxin
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iron-sulfur centre
NADH
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putative nucleotide-binding site in the gamma subunit
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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one mol of HydA contains 7 mol iron
Ni2+
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contains 1 g atoms of Ni per mole of protein
Se
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the large subunit contains a selenocysteine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
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66% activity at 1 mM
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
Acutodesmus obliquus
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inhibition of H2 production, photosystem 1 is involved in the supply of electrons to the hydrogenase
CuSO4
EDTA
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at 0.2 M 35% inhibition of hydrogen production and 27% inhibition of hydrogen oxidation
ethylene glycol
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inhibitory to hydrogen production
guanidine hydrochloride
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at 10 mM inhibitory, hydrogen production
o-phenanthroline
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36% activity at 1 mM
phenylmethanesulfonyl fluoride
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61% activity at 1 mM
Procion red
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competitive inhibition, bidirectional hydrogenase
Sodium mersalyl
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at 12.2 mol per mol protein, 70% inhibition
sulfo-disalicylidinepropandiamine
Acutodesmus obliquus
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hydrogenase activity is reduced up to 30-fold
Tiron
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inhibits methyl viologen hydrogen oxidation
Tris-HCl
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at 30 mM inhibitory, hydrogen production
Urea
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at 10 mM inhibitory, hydrogen production