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Q2NXE2

- ACSA_XANOM

UniProt

Q2NXE2 - ACSA_XANOM

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, XOO4280
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Status
Reviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei310 – 3101Coenzyme A By similarity
Binding sitei334 – 3341Coenzyme A By similarity
Binding sitei386 – 3861Substrate; via amide nitrogen By similarity
Binding sitei499 – 4991Substrate By similarity
Binding sitei514 – 5141Substrate By similarity
Active sitei516 – 5161 By similarity
Binding sitei522 – 5221Coenzyme A By similarity
Binding sitei525 – 5251Substrate By similarity
Metal bindingi536 – 5361Magnesium; via carbonyl oxygen By similarity
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarity
Metal bindingi541 – 5411Magnesium; via carbonyl oxygen By similarity
Binding sitei583 – 5831Coenzyme A

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciXORY342109:GIX9-4339-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
Ordered Locus Names:XOO4280
OrganismiXanthomonas oryzae pv. oryzae (strain MAFF 311018)
Taxonomic identifieri342109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001957: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000085008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei608 – 6081N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi342109.XOO_4280.

Structurei

3D structure databases

ProteinModelPortaliQ2NXE2.
SMRiQ2NXE2. Positions 9-644.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni410 – 4156Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000128470.
KOiK01895.
OMAiRRIFEPT.
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.

Q2NXE2-1 [UniParc]FASTAAdd to Basket

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MADVYPVDPA FAADARVTRE QYAALYRESI EHPEQFWGKA AQRLEWFKQP    50
TQVKDVSYAL DDFHIRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP 100
DAASYPVTYR QLYERVCKLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA 150
CARIGAVHSV VFGGFAANSI ADRVIDCQSK LIITADEGLR GGKKIPLKAN 200
VDAALKIPGT NTIETVLVVR HTGGAVEMQA PRDRWFHDVV DGQPAECEPE 250
RMNAEDPLFI LYTSGSTGKP KGVLHTTAGY LLFASYTHEV VFDLREDDIY 300
WCTADVGWVT GHSYIVYGPL ANGATAVMFE GVPNYPNVSR FWEVIDKHQV 350
TIFYTAPTAI RALMRDGAEP VKKTSRKSLR LLGSVGEPIN PEAWRWYYDV 400
VGDSRCPIVD TWWQTETGGI LISPLAGAVD LKPGSATLPF FGVQPALVDA 450
EGKILEGATE GNLVLLDSWP GQMRSVYGDH QRFIDTYFRT YPGSYFTGDG 500
CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
HDVKGQGIYA YVTLIAGETP SDELHKELVS WVRKEIGPIA SPDHLQWAPG 600
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR 647
Length:647
Mass (Da):71,366
Last modified:February 7, 2006 - v1
Checksum:i33558E37802A2523
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008229 Genomic DNA. Translation: BAE71035.1.
RefSeqiYP_453309.1. NC_007705.1.

Genome annotation databases

EnsemblBacteriaiBAE71035; BAE71035; BAE71035.
GeneIDi3859446.
KEGGixom:XOO_4280.
PATRICi24119017. VBIXanOry49434_4911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008229 Genomic DNA. Translation: BAE71035.1 .
RefSeqi YP_453309.1. NC_007705.1.

3D structure databases

ProteinModelPortali Q2NXE2.
SMRi Q2NXE2. Positions 9-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 342109.XOO_4280.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE71035 ; BAE71035 ; BAE71035 .
GeneIDi 3859446.
KEGGi xom:XOO_4280.
PATRICi 24119017. VBIXanOry49434_4911.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000128470.
KOi K01895.
OMAi RRIFEPT.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci XORY342109:GIX9-4339-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
    Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
    Jpn. Agric. Res. Q. 39:275-287(2005)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MAFF 311018.

Entry informationi

Entry nameiACSA_XANOM
AccessioniPrimary (citable) accession number: Q2NXE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 7, 2006
Last modified: May 14, 2014
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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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