SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

G4REV1

- G4REV1_PELHB

UniProt

G4REV1 - G4REV1_PELHB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acsA, KKY_1911
Organism
Pelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2)
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 sitei309 – 3091Coenzyme A By similarityUniRule annotation
Binding sitei333 – 3331Coenzyme A By similarityUniRule annotation
Binding sitei385 – 3851Substrate; 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. 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

BioCyciPHAL1082931:GJXT-1906-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:KKY_1911Imported
OrganismiPelagibacterium halotolerans (strain JCM 15775 / CGMCC 1.7692 / B2)Imported
Taxonomic identifieri1082931 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaePelagibacterium
ProteomesiUP000008850: 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

ProteinModelPortaliG4REV1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 4146Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.
OMAiQTAILFE.

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.

G4REV1-1 [UniParc]FASTAAdd to Basket

« Hide

MSSEVFAPSD EVVAKTRVTA EQYDRMYRRS VSDPDGFWGE QAQRIDWIKP    50
FTKVKNTSFE WPDVSIKWFE DGQLNVAANC IDRHLKEHGD TVAIIFEPDD 100
PEAETRHITY RLLHGEVCRF ANVLKELGVQ KGERVTIYMP MIPEAAYAML 150
ACARIGAVHS VVFGGFSPDA LAGRVNDCDS RVVITADEGC RGGKKVPLKV 200
NVDKALEDCP GVEKVLVVRN TGSDIAMTSG RDVWLHEAEA GVEAVCEPEP 250
MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL VYASLTHELT FDYRQGEVFW 300
CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPNYPDAGRF WEVVDKHKVN 350
IFYTAPTAIR ALMGAGNQFV ERADLSSLRL LGSVGEPINP EAWMWYHKQV 400
GRERCIVVDT WWQTETGGFM ITPLPGAIPT KPGSATKPFF GVQPVVLEPE 450
SGKVIEETEA AGVLAIADSW PGQMRTVYGD HQRFKETYFQ QYKGYYFTGD 500
GCRRDEDGYY WITGRVDDVL NVSGHRLGTA EVESALVAHP KVSEAAVVGF 550
PHDVKGQGIY CYVTLMAGEA ASDDLAGELR NWVRKEIGPI ASPDHIQFAP 600
GLPKTRSGKI MRRILRKVAE NDYGALGDTS TLADPGVVDD LIANRKNR 648
Length:648
Mass (Da):71,561
Last modified:December 14, 2011 - v1
Checksum:i1940E68026A1A373
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003075 Genomic DNA. Translation: AEQ51922.1.
RefSeqiWP_014131071.1. NC_016078.1.
YP_004899672.1. NC_016078.1.

Genome annotation databases

EnsemblBacteriaiAEQ51922; AEQ51922; KKY_1911.
GeneIDi11342874.
KEGGiphl:KKY_1911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003075 Genomic DNA. Translation: AEQ51922.1 .
RefSeqi WP_014131071.1. NC_016078.1.
YP_004899672.1. NC_016078.1.

3D structure databases

ProteinModelPortali G4REV1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEQ51922 ; AEQ51922 ; KKY_1911 .
GeneIDi 11342874.
KEGGi phl:KKY_1911.

Phylogenomic databases

KOi K01895.
OMAi QTAILFE.

Enzyme and pathway databases

BioCyci PHAL1082931:GJXT-1906-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: JCM 15775 / CGMCC 1.7692 / B2.

Entry informationi

Entry nameiG4REV1_PELHB
AccessioniPrimary (citable) accession number: G4REV1
Entry historyi
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: September 3, 2014
This is version 19 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

Similar proteinsi