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Information on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme and Organism(s) Arabidopsis thaliana

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.23 E2 ubiquitin-conjugating enzyme
IUBMB Comments
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+
[E2 ubiquitin-conjugating enzyme]-L-cysteine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Synonyms
ube2c, cdc34, ubc13, ube2t, ubch10, e2 enzyme, ube2s, ubch7, e2 ubiquitin-conjugating enzyme, ube2l3, more
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
-
-
-
-
?
[ubiquitin-activating protein UBA1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein BA1]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
show the reaction diagram
transfer of ubiquitin from activating protein UBA1 can take place to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
-
-
?
[ubiquitin-activating protein UBA2]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein UBA2]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
show the reaction diagram
transfer of activated ubiquitin from E1 enzyme UBA2 is carried out to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBC5_ARATH
185
0
21179
Swiss-Prot
other Location (Reliability: 3)
UBC6_ARATH
183
0
20785
Swiss-Prot
other Location (Reliability: 2)
UBC7_ARATH
166
0
18722
Swiss-Prot
other Location (Reliability: 3)
UBC13_ARATH
166
0
18822
Swiss-Prot
other Location (Reliability: 4)
UBC14_ARATH
167
0
18728
Swiss-Prot
other Location (Reliability: 3)
UBC15_ARATH
161
0
18262
Swiss-Prot
Chloroplast (Reliability: 5)
UBC16_ARATH
161
0
18485
Swiss-Prot
Chloroplast (Reliability: 5)
UBC17_ARATH
161
0
18674
Swiss-Prot
other Location (Reliability: 4)
UBC18_ARATH
161
0
18372
Swiss-Prot
Chloroplast (Reliability: 4)
UBC30_ARATH
148
0
16480
Swiss-Prot
other Location (Reliability: 3)
UBC31_ARATH
154
0
17833
Swiss-Prot
other Location (Reliability: 4)
UBC32_ARATH
309
1
34322
Swiss-Prot
other Location (Reliability: 3)
UBC33_ARATH
243
1
27357
Swiss-Prot
other Location (Reliability: 5)
UBC34_ARATH
237
1
26614
Swiss-Prot
other Location (Reliability: 5)
UBC35_ARATH
153
0
17192
Swiss-Prot
other Location (Reliability: 5)
UBC36_ARATH
153
0
17220
Swiss-Prot
other Location (Reliability: 5)
UBC37_ARATH
409
0
45083
Swiss-Prot
Mitochondrion (Reliability: 4)
UBC38_ARATH
326
0
37292
Swiss-Prot
other Location (Reliability: 4)
UBC39_ARATH
316
0
36488
Swiss-Prot
other Location (Reliability: 2)
UBC3_ARATH
150
0
17137
Swiss-Prot
other Location (Reliability: 4)
UBC4_ARATH
187
0
21298
Swiss-Prot
other Location (Reliability: 2)
UBC19_ARATH
181
0
19999
Swiss-Prot
Chloroplast (Reliability: 4)
UBC1_ARATH
152
0
17281
Swiss-Prot
Mitochondrion (Reliability: 5)
UBC20_ARATH
180
0
19792
Swiss-Prot
Chloroplast (Reliability: 4)
UBC22_ARATH
251
0
27399
Swiss-Prot
other Location (Reliability: 2)
UBC23_ARATH
1102
0
122183
Swiss-Prot
other Location (Reliability: 2)
UBC24_ARATH
907
0
100484
Swiss-Prot
other Location (Reliability: 2)
UBC25_ARATH
609
0
67769
Swiss-Prot
other Location (Reliability: 4)
UBC26_ARATH
543
0
60552
Swiss-Prot
other Location (Reliability: 3)
UBC27_ARATH
192
0
21254
Swiss-Prot
other Location (Reliability: 2)
UBC28_ARATH
148
0
16510
Swiss-Prot
other Location (Reliability: 2)
UBC29_ARATH
148
0
16759
Swiss-Prot
other Location (Reliability: 3)
UBC2_ARATH
152
0
17279
Swiss-Prot
Mitochondrion (Reliability: 5)
PEX4_ARATH
157
0
17708
Swiss-Prot
other Location (Reliability: 2)
UBC8_ARATH
148
0
16533
Swiss-Prot
other Location (Reliability: 2)
UBC10_ARATH
148
0
16537
Swiss-Prot
other Location (Reliability: 2)
UBC11_ARATH
148
0
16551
Swiss-Prot
other Location (Reliability: 2)
UBC12_ARATH
149
0
16710
Swiss-Prot
other Location (Reliability: 5)
F4KAG5_ARATH
203
0
22601
TrEMBL
other Location (Reliability: 2)
A0A178U7V3_ARATH
192
0
21254
TrEMBL
other Location (Reliability: 2)
UBE12_ARATH
1077
0
119624
Swiss-Prot
Chloroplast (Reliability: 3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hatfield, P.M.; Gosink, M.M.; Carpenter, T.B.; Vierstra, R.D.
The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana
Plant J.
11
213-226
1997
Arabidopsis thaliana, Arabidopsis thaliana (P92974)
Manually annotated by BRENDA team
Unver, T.; Turktas, M.; Budak, H.
In planta evidence for the involvement of a ubiquitin conjugating enzyme (UBI E2 Clade) in negative regulation of disease resistance
Plant Mol. Biol. Rep.
31
323-334
2013
Nicotiana benthamiana, Arabidopsis thaliana (P42745)
-
Manually annotated by BRENDA team
Wen, R.; Wang, S.; Xiang, D.; Venglat, P.; Shi, X.; Zang, Y.; Datla, R.; Xiao, W.; Wang, H.
UBC13, an E2 enzyme for Lys63-linked ubiquitination, functions in root development by affecting auxin signaling and Aux/IAA protein stability
Plant J.
80
424-436
2014
Arabidopsis thaliana (Q94A97)
Manually annotated by BRENDA team
Imura, Y.; Molho, M.; Chuang, C.; Nagy, P.D.
Cellular Ubc2/Rad6 E2 ubiquitin-conjugating enzyme facilitates tombusvirus replication in yeast and plants
Virology
484
265-275
2015
Arabidopsis thaliana, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team