Skip Header

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

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2)
Status
Unreviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei309Coenzyme AUniRule annotation1
Binding sitei333Coenzyme AUniRule annotation1
Binding sitei500ATPUniRule annotation1
Binding sitei515ATPUniRule annotation1
Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei526ATPUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei584Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi385 – 387ATPUniRule annotation3
Nucleotide bindingi409 – 414ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

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

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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:KKY_1911Imported
OrganismiPelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2)Imported
Taxonomic identifieri1082931 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaePelagibacterium
Proteomesi
  • UP000008850 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi1082931.KKY_1911.

Structurei

3D structure databases

ProteinModelPortaliG4REV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 80ACAS_NInterPro annotationAdd BLAST58
Domaini82 – 522AMP-bindingInterPro annotationAdd BLAST441
Domaini531 – 609AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni191 – 194Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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

        10         20         30         40         50
MSSEVFAPSD EVVAKTRVTA EQYDRMYRRS VSDPDGFWGE QAQRIDWIKP
60 70 80 90 100
FTKVKNTSFE WPDVSIKWFE DGQLNVAANC IDRHLKEHGD TVAIIFEPDD
110 120 130 140 150
PEAETRHITY RLLHGEVCRF ANVLKELGVQ KGERVTIYMP MIPEAAYAML
160 170 180 190 200
ACARIGAVHS VVFGGFSPDA LAGRVNDCDS RVVITADEGC RGGKKVPLKV
210 220 230 240 250
NVDKALEDCP GVEKVLVVRN TGSDIAMTSG RDVWLHEAEA GVEAVCEPEP
260 270 280 290 300
MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL VYASLTHELT FDYRQGEVFW
310 320 330 340 350
CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPNYPDAGRF WEVVDKHKVN
360 370 380 390 400
IFYTAPTAIR ALMGAGNQFV ERADLSSLRL LGSVGEPINP EAWMWYHKQV
410 420 430 440 450
GRERCIVVDT WWQTETGGFM ITPLPGAIPT KPGSATKPFF GVQPVVLEPE
460 470 480 490 500
SGKVIEETEA AGVLAIADSW PGQMRTVYGD HQRFKETYFQ QYKGYYFTGD
510 520 530 540 550
GCRRDEDGYY WITGRVDDVL NVSGHRLGTA EVESALVAHP KVSEAAVVGF
560 570 580 590 600
PHDVKGQGIY CYVTLMAGEA ASDDLAGELR NWVRKEIGPI ASPDHIQFAP
610 620 630 640
GLPKTRSGKI MRRILRKVAE NDYGALGDTS TLADPGVVDD LIANRKNR
Length:648
Mass (Da):71,561
Last modified:December 14, 2011 - v1
Checksum:i1940E68026A1A373
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003075 Genomic DNA. Translation: AEQ51922.1.
RefSeqiWP_014131071.1. NC_016078.1.

Genome annotation databases

EnsemblBacteriaiAEQ51922; AEQ51922; KKY_1911.
KEGGiphl:KKY_1911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003075 Genomic DNA. Translation: AEQ51922.1.
RefSeqiWP_014131071.1. NC_016078.1.

3D structure databases

ProteinModelPortaliG4REV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1082931.KKY_1911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEQ51922; AEQ51922; KKY_1911.
KEGGiphl:KKY_1911.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.