GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:SUCC

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) sucC
Protein Name(s) Succinyl-CoA ligase [ADP-forming] subunit beta

Succinyl-CoA synthetase subunit beta SCS-beta

External Links
UniProt P0A836
EMBL J01619
U00096
AP009048
PIR A24090
RefSeq NP_415256.1
YP_489007.1
PDB 1CQI
1CQJ
1JKJ
1JLL
1SCU
2NU6
2NU7
2NU8
2NU9
2NUA
2SCU
PDBsum 1CQI
1CQJ
1JKJ
1JLL
1SCU
2NU6
2NU7
2NU8
2NU9
2NUA
2SCU
ProteinModelPortal P0A836
SMR P0A836
DIP DIP-31852N
IntAct P0A836
STRING 511145.b0728
SWISS-2DPAGE P0A836
PaxDb P0A836
PRIDE P0A836
EnsemblBacteria AAC73822
BAA35394
GeneID 12930952
945312
KEGG ecj:Y75_p0707
eco:b0728
PATRIC 32116651
EchoBASE EB0974
EcoGene EG10981
eggNOG COG0045
HOGENOM HOG000007059
InParanoid P0A836
KO K01903
OMA LCMDAKF
OrthoDB EOG644ZT0
PhylomeDB P0A836
BioCyc EcoCyc:SUCCCOASYN-BETA
ECOL316407:JW0717-MONOMER
MetaCyc:SUCCCOASYN-BETA
UniPathway UPA00223
EvolutionaryTrace P0A836
PRO PR:P0A836
Proteomes UP000000318
UP000000625
Genevestigator P0A836
GO GO:0005737
GO:0009361
GO:0005524
GO:0000287
GO:0030145
GO:0004775
GO:0006099
Gene3D 3.30.1490.20
3.30.470.20
3.40.50.261
HAMAP MF_00558
InterPro IPR011761
IPR013650
IPR013815
IPR013816
IPR005811
IPR017866
IPR005809
IPR016102
PANTHER PTHR11815
Pfam PF08442
PF00549
PIRSF PIRSF001554
SUPFAM SSF52210
TIGRFAMs TIGR01016
PROSITE PS50975
PS01217

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005737

cytoplasm

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:3543212[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004775

succinate-CoA ligase (ADP-forming) activity

PMID:3543212[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009361

succinate-CoA ligase complex (ADP-forming)

PMID:8144675[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005811

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011761
InterPro:IPR013815

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005809

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011761

F

Seeded From UniProt

complete

enables

GO:0004775

succinate-CoA ligase (ADP-forming) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.2.1.5

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101646

F

Seeded From UniProt

complete

enables

GO:0004775

succinate-CoA ligase (ADP-forming) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101646

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101646

F

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101646

P

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0816
UniPathway:UPA00223

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. 2.0 2.1 Buck, D et al. (1986) Cloning and expression of the succinyl-CoA synthetase genes of Escherichia coli K12. J. Gen. Microbiol. 132 1753-62 PubMed GONUTS page
  3. Wolodko, WT et al. (1994) The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. J. Biol. Chem. 269 10883-90 PubMed GONUTS page
  4. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page