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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Status
Reviewed-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 sitei498ATPUniRule annotation1
Binding sitei513ATPUniRule annotation1
Binding sitei521Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei524ATPUniRule annotation1
Metal bindingi535Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi540Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei582Coenzyme 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

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, 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:Xaut_1479
OrganismiXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Taxonomic identifieri78245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter
Proteomesi
  • UP000002417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001372791 – 651Acetyl-coenzyme A synthetaseAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei607N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi78245.Xaut_1479.

Structurei

3D structure databases

ProteinModelPortaliA7IFD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 193Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
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.

A7IFD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKIYYVPS EWAQKAYVDD AHYQSMYAAS VNDPHAFWGE HGKRIDWFTP
60 70 80 90 100
YTKVKNTSFD PGHVSIKWFE DGITNVAYNC VDRHLETRGD QVAIIWEGDS
110 120 130 140 150
PDESRNITYR ELSSEVNKLA NVLRNRGVEK GDRVTIYLPM IPEAAFAMLA
160 170 180 190 200
CARLGAIHSI VFGGFSPDSL AGRVADCGSK CIITADEGLR GGRKVPLKAN
210 220 230 240 250
VDAAIAQING GVDHVIVVRR TGGKVDMLPG RDVYYDEATA MVTDECPAEH
260 270 280 290 300
VNAEDPLFIL YTSGSTGKPK GVLHTTGGYL VYASMTHQYI FDYHPGDIYW
310 320 330 340 350
CTADVGWVTG HSYIVYGPLA NGATTLMFEG IPNYPSVSRF WDVIDKHKVN
360 370 380 390 400
IFYTAPTAIR SLMQAGEEPV KRTSRSSLRL LGSVGEPINP EAWEWYYRVV
410 420 430 440 450
GEERCPIVDT WWQTETGGIL ITPLPGATKL KPGSATRPFF GVMPEVVDAE
460 470 480 490 500
GKVLEGACEG NLVIADSWPG QMRTVYGDHE RFEQTYFSTY PGKYFTGDGC
510 520 530 540 550
RRDADGFYWI TGRVDDVINV SGHRMGTAEV ESALVAHPKV SEAAVVGFPH
560 570 580 590 600
DIKGQGIYAY VTLMDGEEPT EELRKELVGW VRREIGPIAS PDLIQFAPGL
610 620 630 640 650
PKTRSGKIMR RILRKIAEDQ FESLGDTSTL ADPGVVEDLI HNRQNKRDAA

A
Length:651
Mass (Da):72,073
Last modified:September 11, 2007 - v1
Checksum:i78FD976772E3626C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000781 Genomic DNA. Translation: ABS66727.1.
RefSeqiWP_012113500.1. NC_009720.1.

Genome annotation databases

EnsemblBacteriaiABS66727; ABS66727; Xaut_1479.
KEGGixau:Xaut_1479.
PATRICi24044963. VBIXanAut29526_1778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000781 Genomic DNA. Translation: ABS66727.1.
RefSeqiWP_012113500.1. NC_009720.1.

3D structure databases

ProteinModelPortaliA7IFD4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi78245.Xaut_1479.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS66727; ABS66727; Xaut_1479.
KEGGixau:Xaut_1479.
PATRICi24044963. VBIXanAut29526_1778.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
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 nameiACSA_XANP2
AccessioniPrimary (citable) accession number: A7IFD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 11, 2007
Last modified: November 2, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.