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B2FNG6

- B2FNG6_STRMK

UniProt

B2FNG6 - B2FNG6_STRMK

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Smlt4623
Organism
Stenotrophomonas maltophilia (strain K279a)
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. 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

LigaseUniRule annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciSMAL522373:GJE8-4460-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:Smlt4623Imported
OrganismiStenotrophomonas maltophilia (strain K279a)Imported
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840: 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

STRINGi522373.Smlt4623.

Structurei

3D structure databases

ProteinModelPortaliB2FNG6.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiHPPQKML.
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.

B2FNG6-1 [UniParc]FASTAAdd to Basket

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MADIYPVDPQ FAAKARIDKT SYEQQYQASV TDPDGFWGKA AERLQWMRKP    50
TRIKNVSYDL SDFHIKWFED GELNASVNCL DRQLETRGDK TALLFEPDGP 100
DAPAQHVTYR ELYERTCRLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA 150
CARIGAIHSV VFGGFAPNSI ADRVSDCQSK LIITADEGLR GGRRIPLKAN 200
VDAALKLPGT NTVETVLVVR HTGGAVDMQA PRDRWFHDVV DSQPATCEPE 250
RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLYAAYTHEA VFDLREDDIY 300
WCTADVGWVT GHSYIVYGPL ANGATSLMFE GVPNYPDTSR FWNVIDKHKV 350
TIFYTAPTAI RALMREGEEP VKKTSRASLR LLGSVGEPIN PEAWRWYYEV 400
VGDSRCPIVD TWWQTETGGI LISPLAGAMD LKPGSATLPF FGVQPALVNA 450
DGEIQDGPTE GNLIIRDSWP GQMRTVYGDH QRFIDTYFRT YPGSYFTGDG 500
CRRDEDGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
HDVKGQGIYA YVTLVAEEAP SDELHKELIA WVRKEIGPIA TPDHLQWAPG 600
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVASL VDERKVR 647
Length:647
Mass (Da):71,696
Last modified:June 10, 2008 - v1
Checksum:i309006DBC8BA7090
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ47977.1.
RefSeqiYP_001974253.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ47977; CAQ47977; Smlt4623.
GeneIDi6392775.
KEGGisml:Smlt4623.
PATRICi23704627. VBISteMal45202_4358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ47977.1 .
RefSeqi YP_001974253.1. NC_010943.1.

3D structure databases

ProteinModelPortali B2FNG6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 522373.Smlt4623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ47977 ; CAQ47977 ; Smlt4623 .
GeneIDi 6392775.
KEGGi sml:Smlt4623.
PATRICi 23704627. VBISteMal45202_4358.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SMAL522373:GJE8-4460-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. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279aImported.

Entry informationi

Entry nameiB2FNG6_STRMK
AccessioniPrimary (citable) accession number: B2FNG6
Entry historyi
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 43 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

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