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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei309 – 3091Coenzyme AUniRule annotation
Binding sitei333 – 3331Coenzyme AUniRule annotation
Binding sitei498 – 4981ATPUniRule annotation
Binding sitei513 – 5131ATPUniRule annotation
Binding sitei521 – 5211Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei524 – 5241ATPUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei582 – 5821Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi385 – 3873ATPUniRule annotation
Nucleotide bindingi409 – 4146ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciXAUT78245:GHS6-1493-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: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_1000137279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei607 – 6071N6-acetyllysineUniRule annotation

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.
SMRiA7IFD4. Positions 8-644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
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.
SMRiA7IFD4. Positions 8-644.
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.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciXAUT78245:GHS6-1493-MONOMER.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1158 / Py2.

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 11, 2015
This is version 57 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.