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D7A5Y5

- D7A5Y5_STAND

UniProt

D7A5Y5 - D7A5Y5_STAND

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, Snov_2812
Organism
Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113)
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 sitei310 – 3101Coenzyme A By similarityUniRule annotation
Binding sitei334 – 3341Coenzyme A By similarityUniRule annotation
Binding sitei386 – 3861Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei499 – 4991Substrate By similarityUniRule annotation
Binding sitei514 – 5141Substrate By similarityUniRule annotation
Active sitei516 – 5161 By similarityUniRule annotation
Binding sitei522 – 5221Coenzyme A By similarityUniRule annotation
Binding sitei525 – 5251Substrate By similarityUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei583 – 5831Coenzyme 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 annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciSNOV639283:GCS4-2845-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:Snov_2812Imported
OrganismiStarkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113)Imported
Taxonomic identifieri639283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeStarkeya
ProteomesiUP000006633: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei608 – 6081N6-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

ProteinModelPortaliD7A5Y5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni410 – 4156Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

D7A5Y5-1 [UniParc]FASTAAdd to Basket

« Hide

MSDKIYDVPA EWAKRAFLNE HAYRAKYEAS VRDTEGFWAE EGKRIEWFEP    50
YTIVKNTSYD PGHVSIKWFE DGVTNVAWNC IDRHLPRLAD QTAIIWEGDD 100
PSQSRHITYQ ELHDEVCRFA NVLRNRNVEK GDRVTIYMPM IPEAAYAMLA 150
CARLGAIHSV VFGGFSPDSL AGRIRDCGSK VIITADEGLR GGRKVPLKAN 200
VDAAIAKVSD VEIDHVIVVK RTGGEVDMKP GRDVWYHQAA DLVTSECPAV 250
PMNAEDPLFI LYTSGSTGLP KGVLHTTGGY LVYASMTHQY VFDYHDGDVY 300
WCTADIGWVT GHSYIVYGPL ANGATTLMFE GVPNYPSNSR FWEVIDKHKV 350
NIFYTAPTAI RALMQAGDEP VKKTSRASLR LLGSVGEPIN PEAWEWYHRV 400
VGEDRCPIVD TWWQTETGGI LITPLPGATR LKPGSATQPF FGVIPQVVDA 450
EGRVLEGACE GNLVIADSWP GQMRTVYGDH ERFMQTYFAT YPGKYFTGDG 500
CRRDSDGYYW ITGRVDDVIN VSGHRMGTAE VESALVAHPK VSEAAVVGYP 550
HDIKGQGIYA YVTLMAGAEP TEELRKELVA WVRREIGPIA SPDLIQFAPS 600
LPKTRSGKIM RRILRKIAED EFGNLGDTST LADPTVVQDL ISQRQNKKHA 650
AA 652
Length:652
Mass (Da):72,499
Last modified:August 10, 2010 - v1
Checksum:i1A1A1258EB1694A6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002026 Genomic DNA. Translation: ADH90100.1.
RefSeqiWP_013167604.1. NC_014217.1.
YP_003694719.1. NC_014217.1.

Genome annotation databases

EnsemblBacteriaiADH90100; ADH90100; Snov_2812.
GeneIDi9333895.
KEGGisno:Snov_2812.
PATRICi38258209. VBIStaNov45716_2813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002026 Genomic DNA. Translation: ADH90100.1 .
RefSeqi WP_013167604.1. NC_014217.1.
YP_003694719.1. NC_014217.1.

3D structure databases

ProteinModelPortali D7A5Y5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADH90100 ; ADH90100 ; Snov_2812 .
GeneIDi 9333895.
KEGGi sno:Snov_2812.
PATRICi 38258209. VBIStaNov45716_2813.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci SNOV639283:GCS4-2845-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: ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113.

Entry informationi

Entry nameiD7A5Y5_STAND
AccessioniPrimary (citable) accession number: D7A5Y5
Entry historyi
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: September 3, 2014
This is version 29 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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