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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei359 – 3591Coenzyme AUniRule annotation
Binding sitei383 – 3831Coenzyme AUniRule annotation
Binding sitei548 – 5481ATPUniRule annotation
Binding sitei563 – 5631ATPUniRule annotation
Binding sitei571 – 5711Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei574 – 5741ATPUniRule annotation
Metal bindingi585 – 5851Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi587 – 5871Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi590 – 5901Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei632 – 6321Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi435 – 4373ATPUniRule annotation
Nucleotide bindingi459 – 4646ATPUniRule annotation

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

Enzyme and pathway databases

BioCyciXORY291331:GJBV-4197-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:XOO4544Imported
OrganismiXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)Imported
Taxonomic identifieri291331 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000006735 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei657 – 6571N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5GU25.
SMRiQ5GU25. Positions 58-693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni239 – 2424Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiMRHTDCL.
OrthoDBiEOG68WR2H.

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.

Q5GU25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAGALPGGL RPRSKAPLAV GTEWMRHTDC LPREAVTPSS DKFIASEGAM
60 70 80 90 100
ADVYPVDPAF AADARVTREQ YAALYRESIE HPEQFWGKAA QRLEWFKQPT
110 120 130 140 150
QVKDVSYALD DFHIRWFGDG ELNASVNCLD RQLATRGDKT ALLFEPDSPD
160 170 180 190 200
AASYPVTYRQ LYERVCKLGN ALRNLGVKKG DRVTIYLPMI VDAAVAMLAC
210 220 230 240 250
ARIGAVHSVV FGGFAANSIA DRVIDCQSKL IITADEGLRG GKKIPLKANV
260 270 280 290 300
DAALKIPGTN TIETVLVVRH TGGAVEMQAP RDRWFQDVVD GQPAECEPER
310 320 330 340 350
MNAEDPLFIL YTSGSTGKPK GVLHTTAGYL LFASYTHEVV FDLREDDIYW
360 370 380 390 400
CTADVGWVTG HSYIVYGPLA NGATAVMFEG VPNYPNVSRF WEVIDKHQVT
410 420 430 440 450
IFYTAPTAIR ALMRDGAEPV KKTSRKSLRL LGSVGEPINP EAWRWYYDVV
460 470 480 490 500
GDSRCPIVDT WWQTETGGIL ISPLAGAVDL KPGSATLPFF GVQPALVDAE
510 520 530 540 550
GKILEGATEG NLVLLDSWPG QMRSVYGDHQ RFIDTYFRTY PGSYFTGDGC
560 570 580 590 600
RRDADGYYWI TGRVDDVINV SGHRIGTAEV ESALVSHPKV AEAAVVGFPH
610 620 630 640 650
DVKGQGIYAY VTLIAGETPS DELHKELVSW VRKEIGPIAS PDHLQWAPGL
660 670 680 690
PKTRSGKIMR RILRKIAENA PDQLGDTSTL ADPSVVDSLV NERLTR
Length:696
Mass (Da):76,479
Last modified:March 1, 2005 - v1
Checksum:i79025F1A1D84B06A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013598 Genomic DNA. Translation: AAW77798.1.
RefSeqiWP_011260815.1. NC_006834.1.
YP_203183.1. NC_006834.1.

Genome annotation databases

EnsemblBacteriaiAAW77798; AAW77798; XOO4544.
KEGGixoo:XOO4544.
PATRICi24108869. VBIXanOry111333_5045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013598 Genomic DNA. Translation: AAW77798.1.
RefSeqiWP_011260815.1. NC_006834.1.
YP_203183.1. NC_006834.1.

3D structure databases

ProteinModelPortaliQ5GU25.
SMRiQ5GU25. Positions 58-693.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW77798; AAW77798; XOO4544.
KEGGixoo:XOO4544.
PATRICi24108869. VBIXanOry111333_5045.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiMRHTDCL.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciXORY291331:GJBV-4197-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KACC10331 / KXO85Imported.

Entry informationi

Entry nameiQ5GU25_XANOR
AccessioniPrimary (citable) accession number: Q5GU25
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: June 24, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.