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Q2NXE2

- ACSA_XANOM

UniProt

Q2NXE2 - ACSA_XANOM

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Status
Reviewed - 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

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei310 – 3101Coenzyme AUniRule annotation
Binding sitei334 – 3341Coenzyme AUniRule annotation
Binding sitei499 – 4991ATPUniRule annotation
Binding sitei514 – 5141ATPUniRule annotation
Binding sitei522 – 5221Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei525 – 5251ATPUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei583 – 5831Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi386 – 3883ATPUniRule annotation
Nucleotide bindingi410 – 4156ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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 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: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 synthetasePRO_1000085008Add
BLAST

Amino acid modifications

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

STRINGi342109.XOO_4280.

Structurei

3D structure databases

ProteinModelPortaliQ2NXE2.
SMRiQ2NXE2. Positions 9-644.
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

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

« Hide

        10         20         30         40         50
MADVYPVDPA FAADARVTRE QYAALYRESI EHPEQFWGKA AQRLEWFKQP
60 70 80 90 100
TQVKDVSYAL DDFHIRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP
110 120 130 140 150
DAASYPVTYR QLYERVCKLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA
160 170 180 190 200
CARIGAVHSV VFGGFAANSI ADRVIDCQSK LIITADEGLR GGKKIPLKAN
210 220 230 240 250
VDAALKIPGT NTIETVLVVR HTGGAVEMQA PRDRWFHDVV DGQPAECEPE
260 270 280 290 300
RMNAEDPLFI LYTSGSTGKP KGVLHTTAGY LLFASYTHEV VFDLREDDIY
310 320 330 340 350
WCTADVGWVT GHSYIVYGPL ANGATAVMFE GVPNYPNVSR FWEVIDKHQV
360 370 380 390 400
TIFYTAPTAI RALMRDGAEP VKKTSRKSLR LLGSVGEPIN PEAWRWYYDV
410 420 430 440 450
VGDSRCPIVD TWWQTETGGI LISPLAGAVD LKPGSATLPF FGVQPALVDA
460 470 480 490 500
EGKILEGATE GNLVLLDSWP GQMRSVYGDH QRFIDTYFRT YPGSYFTGDG
510 520 530 540 550
CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP
560 570 580 590 600
HDVKGQGIYA YVTLIAGETP SDELHKELVS WVRKEIGPIA SPDHLQWAPG
610 620 630 640
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR
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: October 1, 2014
This is version 58 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