SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B2SU07

- B2SU07_XANOP

UniProt

B2SU07 - B2SU07_XANOP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acetyl-coenzyme A synthetase

Gene
acsA, PXO_03257
Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

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

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciXORY360094:GI45-5032-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotationImported
Ordered Locus Names:PXO_03257Imported
OrganismiXanthomonas oryzae pv. oryzae (strain PXO99A)Imported
Taxonomic identifieri360094 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001740: Chromosome

PTM / Processingi

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi360094.PXO_03257.

Structurei

3D structure databases

ProteinModelPortaliB2SU07.
SMRiB2SU07. Positions 9-644.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiTGSEVPW.
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.

B2SU07-1 [UniParc]FASTAAdd to Basket

« Hide

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:July 1, 2008 - v1
Checksum:i33558E37802A2523
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000967 Genomic DNA. Translation: ACD61559.1.
RefSeqiYP_001916091.1. NC_010717.1.

Genome annotation databases

EnsemblBacteriaiACD61559; ACD61559; PXO_03257.
GeneIDi6308552.
KEGGixop:PXO_03257.
PATRICi24129651. VBIXanOry73153_5152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000967 Genomic DNA. Translation: ACD61559.1 .
RefSeqi YP_001916091.1. NC_010717.1.

3D structure databases

ProteinModelPortali B2SU07.
SMRi B2SU07. Positions 9-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360094.PXO_03257.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD61559 ; ACD61559 ; PXO_03257 .
GeneIDi 6308552.
KEGGi xop:PXO_03257.
PATRICi 24129651. VBIXanOry73153_5152.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi TGSEVPW.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci XORY360094:GI45-5032-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PXO99AImported.

Entry informationi

Entry nameiB2SU07_XANOP
AccessioniPrimary (citable) accession number: B2SU07
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: June 11, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi