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Q02FT9

- Q02FT9_PSEAB

UniProt

Q02FT9 - Q02FT9_PSEAB

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Protein
Acetyl-coenzyme A synthetase
Gene
acsB, acsA, PA14_62630
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei308 – 3081Coenzyme A By similarityUniRule annotation
Binding sitei332 – 3321Coenzyme A By similarityUniRule annotation
Binding sitei384 – 3841Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei497 – 4971Substrate By similarityUniRule annotation
Binding sitei512 – 5121Substrate By similarityUniRule annotation
Active sitei514 – 5141 By similarityUniRule annotation
Binding sitei520 – 5201Coenzyme A By similarityUniRule annotation
Binding sitei523 – 5231Substrate By similarityUniRule annotation
Metal bindingi534 – 5341Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei581 – 5811Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciPAER208963:GI5K-5113-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsBImported
Synonyms:acsAUniRule annotation
Ordered Locus Names:PA14_62630Imported
OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)Imported
Taxonomic identifieri208963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000653: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei606 – 6061N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi208963.PA14_62630.

Structurei

3D structure databases

ProteinModelPortaliQ02FT9.
SMRiQ02FT9. Positions 7-642.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni408 – 4136Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiRRIFEPT.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02FT9-1 [UniParc]FASTAAdd to Basket

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MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF    50
KPWHSVHHGD LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN 100
PSESAHITYR KLHHNVCRLA NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA 150
CARIGAVHSV VFGGFSPDSL RDRILDADCR TVITADEGVR GGKYIPLKQN 200
VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA ASADCPAEAM 250
DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC 300
TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI 350
FYTAPTAIRA LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG 400
EKRCPIVDTW WQTETGSILI TPLPGATALK PGSATRPFFG VQPVLLDEKG 450
KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR MIDTYFKPYP GYYFSGDGAR 500
RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA EAAVVGCPHD 550
VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP 600
KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR 645
Length:645
Mass (Da):71,640
Last modified:November 14, 2006 - v1
Checksum:iD3F63891F880B1EA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000438 Genomic DNA. Translation: ABJ14116.1.
RefSeqiYP_793197.1. NC_008463.1.

Genome annotation databases

EnsemblBacteriaiABJ14116; ABJ14116; PA14_62630.
GeneIDi4383182.
KEGGipau:PA14_62630.
PATRICi19856442. VBIPseAer79785_5138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000438 Genomic DNA. Translation: ABJ14116.1 .
RefSeqi YP_793197.1. NC_008463.1.

3D structure databases

ProteinModelPortali Q02FT9.
SMRi Q02FT9. Positions 7-642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208963.PA14_62630.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ14116 ; ABJ14116 ; PA14_62630 .
GeneIDi 4383182.
KEGGi pau:PA14_62630.
PATRICi 19856442. VBIPseAer79785_5138.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi RRIFEPT.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci PAER208963:GI5K-5113-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UCBPP-PA14Imported.

Entry informationi

Entry nameiQ02FT9_PSEAB
AccessioniPrimary (citable) accession number: Q02FT9
Entry historyi
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: June 11, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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