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

acs

Organism
Prochlorococcus marinus (strain MIT 9301)
Status
Unreviewed-Annotation score: -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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei322Coenzyme AUniRule annotation1
Binding sitei516ATPUniRule annotation1
Binding sitei531ATPUniRule annotation1
Binding sitei539Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei542ATPUniRule annotation1
Metal bindingi553Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi555Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi558Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi398 – 400ATPUniRule annotation3
Nucleotide bindingi422 – 427ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationImported
LigandATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciPMAR167546:G1G8B-638-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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsImported
Synonyms:acsAUniRule annotation
Ordered Locus Names:P9301_06451Imported
OrganismiProchlorococcus marinus (strain MIT 9301)Imported
Taxonomic identifieri167546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001430 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei625N6-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

STRINGi167546.P9301_06451

Structurei

3D structure databases

ProteinModelPortaliA3PBZ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 92ACAS_NInterPro annotationAdd BLAST53
Domaini102 – 538AMP-bindingInterPro annotationAdd BLAST437
Domaini547 – 625AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni202 – 205Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF Bacteria
COG0365 LUCA
HOGENOMiHOG000229981
KOiK01895
OMAiDHWWHDL
OrthoDBiPOG091H059D

Family and domain databases

CDDicd05966 ACS, 1 hit
HAMAPiMF_01123 Ac_CoA_synth, 1 hit
InterProiView protein in InterPro
IPR011904 Ac_CoA_lig
IPR032387 ACAS_N
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF16177 ACAS_N, 1 hit
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR02188 Ac_CoA_lig_AcsA, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

Sequencei

Sequence statusi: Complete.

A3PBZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ
60 70 80 90 100
FWESFAKSEL DWFEPFQTVL DNENAPFFKW FKEGKLNITY NCLDRHIKRG
110 120 130 140 150
LGGKTALIWE GEPGDSKKYT YEELLKEVCR AANALKAIGV KKGDLVCIYM
160 170 180 190 200
PMIPEAMFAM LACARIGAPH SVVFGGFSSE ALKDRLIDGN ARYVITADGG
210 220 230 240 250
FRKDKVIELK QAVDAAIENG ADKVVEKVVV VQRTKKNISM VDDRDLWWHE
260 270 280 290 300
LVKDQKDQCE PEIMSSEDRL FILYTSGSTG KPKGVVHTTG GYNLWSHLTF
310 320 330 340 350
KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRRSNL
360 370 380 390 400
GAFWEIVQKY KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP
410 420 430 440 450
INPEAWMWYK DVIGKDKCPI VDTWWQTETG GVMISPLPGV VATKPGSATF
460 470 480 490 500
PLPGIEVEIV DKDGDKVKEN EGGYLIIKKP WPGMMRTIHG NSKRYLESYW
510 520 530 540 550
EYISFKGEKN VYFAGDGARI DEDGYIWIMG RVDDVISVSG HRLGTMEIES
560 570 580 590 600
ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVEDLKKHVV
610 620 630 640 650
NEIGIIAKPE KIIISDSLPK TRSGKIMRRI LRSLAGGEKI SGDISTLEDS
660
SVLEKLKELS
Length:660
Mass (Da):74,035
Last modified:April 3, 2007 - v1
Checksum:i8EC977BFDFF2C40D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000576 Genomic DNA Translation: ABO17268.1
RefSeqiWP_011862635.1, NC_009091.1

Genome annotation databases

EnsemblBacteriaiABO17268; ABO17268; P9301_06451
GeneIDi4911088
KEGGipmg:P9301_06451

Similar proteinsi

Entry informationi

Entry nameiA3PBZ3_PROM0
AccessioniPrimary (citable) accession number: A3PBZ3
Entry historyiIntegrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: March 28, 2018
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health