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MYCTU:PCC5

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) accD5 (synonyms: pccB)
Protein Name(s) Probable propionyl-CoA carboxylase beta chain 5

PCCase Propanoyl-CoA:carbon dioxide ligase

External Links
UniProt P9WQH7
EMBL AL123456
PIR A70980
RefSeq NP_217797.1
YP_006516757.1
PDB 2A7S
2BZR
PDBsum 2A7S
2BZR
ProteinModelPortal P9WQH7
SMR P9WQH7
GeneID 13318103
888725
KEGG mtu:Rv3280
mtv:RVBD_3280
TubercuList Rv3280
KO K01966
OMA GLVCNQP
PhylomeDB P9WQH7
UniPathway UPA00945
Proteomes UP000001584
GO GO:0009317
GO:0005618
GO:0005886
GO:0043234
GO:0003989
GO:0005524
GO:0004658
GO:0015977
Gene3D 3.90.226.10
InterPro IPR000022
IPR029045
IPR011763
IPR011762
Pfam PF01039
SUPFAM SSF52096
PROSITE PS50989
PS50980

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004658

propionyl-CoA carboxylase activity

PMID:16354663[1]

ECO:0000314

F

complete

part_of

GO:0005886

plasma membrane

PMID:14532352[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:20825248[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:16385038[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P96886
UniProtKB:P96890

C

Seeded From UniProt

complete

involved_in

GO:0015977

carbon fixation

PMID:16354663[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009317

acetyl-CoA carboxylase complex

PMID:16354663[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004658

propionyl-CoA carboxylase activity

PMID:16354663[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003989

acetyl-CoA carboxylase activity

PMID:16354663[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17157300[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P9WQH7

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16492739[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P9WQH7

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011763

F

Seeded From UniProt

complete

enables

GO:0004658

propionyl-CoA carboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.4.1.3

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: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

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Oh, TJ et al. (2006) Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. J. Biol. Chem. 281 3899-908 PubMed GONUTS page
  2. Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
  3. Wolfe, LM et al. (2010) Proteomic definition of the cell wall of Mycobacterium tuberculosis. J. Proteome Res. 9 5816-26 PubMed GONUTS page
  4. Gago, G et al. (2006) Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J. Bacteriol. 188 477-86 PubMed GONUTS page
  5. Holton, SJ et al. (2006) Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett. 580 6898-902 PubMed GONUTS page
  6. Lin, TW et al. (2006) Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 103 3072-7 PubMed GONUTS page