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F4DQJ9

- F4DQJ9_PSEMN

UniProt

F4DQJ9 - F4DQJ9_PSEMN

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, MDS_3395
Organism
Pseudomonas mendocina (strain NK-01)
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 sitei311 – 3111Coenzyme A By similarityUniRule annotation
Binding sitei335 – 3351Coenzyme A By similarityUniRule annotation
Binding sitei387 – 3871Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei500 – 5001Substrate By similarityUniRule annotation
Binding sitei515 – 5151Substrate By similarityUniRule annotation
Active sitei517 – 5171 By similarityUniRule annotation
Binding sitei523 – 5231Coenzyme A By similarityUniRule annotation
Binding sitei526 – 5261Substrate By similarityUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei584 – 5841Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

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

BioCyciPMEN1001585:GIWS-3446-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:acsAUniRule annotation
Ordered Locus Names:MDS_3395Imported
OrganismiPseudomonas mendocina (strain NK-01)Imported
Taxonomic identifieri1001585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000008306: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-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

Structurei

3D structure databases

ProteinModelPortaliF4DQJ9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.
OMAiDISWING.

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.

F4DQJ9-1 [UniParc]FASTAAdd to Basket

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MSAASLYPVR PEVAARTLTD EATYKAMYQQ SVVNPEGFWR EQGKRIDWIK    50
PYTKVKQTTF DDHHVDIKWY ADGTLNVSYN CLDRHLEERG DQVAIIWEGD 100
DPSEHREITY RQLHEEVSKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML 150
ACARIGAIHS VVFGGFSPEA LAGRIIDCES KVVITADEGL RGGRKVPLKA 200
NVDDALTNPE TASVQKIIVV KRTGSDIKWN QHRDIWYEDL MKVAGSVCAP 250
KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLTYASLTHE RVFDYRPGEV 300
FWCTADIGWV TGHTYLVYGP LSNGATTLMF EGVPNYPDVR RVAQIVDKHK 350
VNILYTAPTA IRAMMAEGKA AVEGADGSSL RLLGSVGEPI NPEAWQWYYE 400
NVGQSRCPIV DTWWQTETGA CLMTPLPGAH GLKPGSAARP FFGVQPALVD 450
NLGNIIEGPA EGNLVIIDSW PGQARTLYGD HDRFVDTYFK TFRGMYFTGD 500
GARRDEDGYW WITGRVDDVL NVSGHRMGTA EVESAMVAHP KVAEAAVVGV 550
PHDIKGQGIY VYVTLNAGEE SSEQLRQELK NWVRKEIGPI ATPDVIQWAP 600
GLPKTRSGKI MRRILRKIAT AEYDSLGDIS TLADPGVVQH LIDTHRQMQA 650
ACA 653
Length:653
Mass (Da):72,265
Last modified:June 28, 2011 - v1
Checksum:iFAD6AE26483A4D3D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1.
RefSeqiYP_004381178.1. NC_015410.1.

Genome annotation databases

EnsemblBacteriaiAEB59426; AEB59426; MDS_3395.
GeneIDi10458177.
KEGGipmk:MDS_3395.
PATRICi54487546. VBIPseMen187712_3448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1 .
RefSeqi YP_004381178.1. NC_015410.1.

3D structure databases

ProteinModelPortali F4DQJ9.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEB59426 ; AEB59426 ; MDS_3395 .
GeneIDi 10458177.
KEGGi pmk:MDS_3395.
PATRICi 54487546. VBIPseMen187712_3448.

Phylogenomic databases

KOi K01895.
OMAi DISWING.

Enzyme and pathway databases

BioCyci PMEN1001585:GIWS-3446-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. "Complete genome of Pseudomonas mendocina NK-01, which synthesizes medium-chain-length polyhydroxyalkanoates and alginate oligosaccharides."
    Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., Song D., Yang X., Wang S.
    J. Bacteriol. 193:3413-3414(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NK-01Imported.

Entry informationi

Entry nameiF4DQJ9_PSEMN
AccessioniPrimary (citable) accession number: F4DQJ9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 2014
This is version 18 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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