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B2FNG6

- B2FNG6_STRMK

UniProt

B2FNG6 - B2FNG6_STRMK

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotationSAAS 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

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi522373.Smlt4623.

Structurei

3D structure databases

ProteinModelPortaliB2FNG6.
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.
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

« Hide

        10         20         30         40         50
MADIYPVDPQ FAAKARIDKT SYEQQYQASV TDPDGFWGKA AERLQWMRKP
60 70 80 90 100
TRIKNVSYDL SDFHIKWFED GELNASVNCL DRQLETRGDK TALLFEPDGP
110 120 130 140 150
DAPAQHVTYR ELYERTCRLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA
160 170 180 190 200
CARIGAIHSV VFGGFAPNSI ADRVSDCQSK LIITADEGLR GGRRIPLKAN
210 220 230 240 250
VDAALKLPGT NTVETVLVVR HTGGAVDMQA PRDRWFHDVV DSQPATCEPE
260 270 280 290 300
RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLYAAYTHEA VFDLREDDIY
310 320 330 340 350
WCTADVGWVT GHSYIVYGPL ANGATSLMFE GVPNYPDTSR FWNVIDKHKV
360 370 380 390 400
TIFYTAPTAI RALMREGEEP VKKTSRASLR LLGSVGEPIN PEAWRWYYEV
410 420 430 440 450
VGDSRCPIVD TWWQTETGGI LISPLAGAMD LKPGSATLPF FGVQPALVNA
460 470 480 490 500
DGEIQDGPTE GNLIIRDSWP GQMRTVYGDH QRFIDTYFRT YPGSYFTGDG
510 520 530 540 550
CRRDEDGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP
560 570 580 590 600
HDVKGQGIYA YVTLVAEEAP SDELHKELIA WVRKEIGPIA TPDHLQWAPG
610 620 630 640
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVASL VDERKVR
Length:647
Mass (Da):71,696
Last modified:June 10, 2008 - v1
Checksum:i309006DBC8BA7090
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 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, Reference proteomeImported

External Data

Dasty 3