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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas putida (strain GB-1)
Status
Unreviewed-Annotation score: 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

Mg2+UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei307 – 3071Coenzyme AUniRule annotation
Binding sitei331 – 3311Coenzyme AUniRule annotation
Binding sitei496 – 4961ATPUniRule annotation
Binding sitei511 – 5111ATPUniRule annotation
Binding sitei519 – 5191Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei522 – 5221ATPUniRule annotation
Metal bindingi533 – 5331Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi383 – 3853ATPUniRule annotation
Nucleotide bindingi407 – 4126ATPUniRule 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

BioCyciPPUT76869:GIXB-4782-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:PputGB1_4701Imported
OrganismiPseudomonas putida (strain GB-1)Imported
Taxonomic identifieri76869 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002157: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei605 – 6051N6-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

STRINGi76869.PputGB1_4701.

Structurei

3D structure databases

ProteinModelPortaliB0KHW7.
SMRiB0KHW7. Positions 21-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWEWYFE.
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.

B0KHW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDIRNYPQA LAVSQSATPT PDEYHRLYRQ SVDDPDTFWA EQAKRLDWIK
60 70 80 90 100
PWSSVQQCDL NTGKARWFDG AQLNVSYNCI DRHLAQRGEQ TALLWEGDDP
110 120 130 140 150
KDSKAITYRE LHRQVCRLAN AMKARGVKKG DRVCIYMPMI PEAAFAMLAC
160 170 180 190 200
TRIGAIHSVV FGGFSPDALR DRILDADCRT VITADEGVRG GKRVPLKQNV
210 220 230 240 250
DKALASCPAV SSVLVVRRTG GDVAWAEGRD LWYHEVTEKA GDDCPPEPMA
260 270 280 290 300
AEDPLFILYT SGSTGKPKGV LHTTGGYLLQ ATMTFKVVFD YRDGEVFWCT
310 320 330 340 350
ADVGWVTGHS YIVYGPLANG AISLMFEGVP NYPDTSRFWQ VVDKHQVNIF
360 370 380 390 400
YTAPTALRAL MREGSAPLQG TSRKSLRLLG SVGEPINPEA WEWYFEAVGQ
410 420 430 440 450
KRCPIVDTWW QTETGGIMLT PLPGSQALKP GCATQPMFGV QPALLDEKGK
460 470 480 490 500
LIEGPGAGLL VIKASWPGQI RSVYGDHQRM VDTYFKPMPG YYFTGDGARR
510 520 530 540 550
DADGDYWITG RIDDVINVSG HRIGTAEVES ALVLHDSVAE AAVVGYPHDL
560 570 580 590 600
KGQGVYAFVT TMNGVTPDDT LKAELLALVS KEIGSFAKPE LIQWAPALPK
610 620 630 640
TRSGKIMRRI LRKIACNELD NLGDTSTLAD PSVVQGLIDK RLNQ
Length:644
Mass (Da):71,051
Last modified:March 18, 2008 - v1
Checksum:i6DA55322F09A7A93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000926 Genomic DNA. Translation: ABZ00588.1.
RefSeqiYP_001670923.1. NC_010322.1.

Genome annotation databases

EnsemblBacteriaiABZ00588; ABZ00588; PputGB1_4701.
GeneIDi5872512.
KEGGippg:PputGB1_4701.
PATRICi19936495. VBIPsePut76638_4709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000926 Genomic DNA. Translation: ABZ00588.1.
RefSeqiYP_001670923.1. NC_010322.1.

3D structure databases

ProteinModelPortaliB0KHW7.
SMRiB0KHW7. Positions 21-641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi76869.PputGB1_4701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABZ00588; ABZ00588; PputGB1_4701.
GeneIDi5872512.
KEGGippg:PputGB1_4701.
PATRICi19936495. VBIPsePut76638_4709.

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWEWYFE.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciPPUT76869:GIXB-4782-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GB-1Imported.

Entry informationi

Entry nameiB0KHW7_PSEPG
AccessioniPrimary (citable) accession number: B0KHW7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 18, 2008
Last sequence update: March 18, 2008
Last modified: March 4, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.