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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas stutzeri CCUG 29243
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 annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei311Coenzyme AUniRule annotation1
Binding sitei335Coenzyme AUniRule annotation1
Binding sitei500ATPUniRule annotation1
Binding sitei515ATPUniRule annotation1
Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei526ATPUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei584Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi387 – 389ATPUniRule annotation3
Nucleotide bindingi411 – 416ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

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

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
ORF Names:A458_12170Imported
OrganismiPseudomonas stutzeri CCUG 29243Imported
Taxonomic identifieri1196835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000006063 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliI4CUB2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 81ACAS_NInterPro annotationAdd BLAST58
Domaini83 – 522AMP-bindingInterPro annotationAdd BLAST440
Domaini531 – 609AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni191 – 194Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

KOiK01895.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

I4CUB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR
60 70 80 90 100
PFTEVKRTSF DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD
110 120 130 140 150
DPSEHREITY RELHQEVSKF ANALRGQDVH RGDVVTIYMP MIPEAAVAML
160 170 180 190 200
ACARIGAIHS VVFGGFSPEA LAGRIIDGQS KIVITADEGV RGGKPVPLKG
210 220 230 240 250
NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL MRVAGEVCAP
260 270 280 290 300
KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV
310 320 330 340 350
YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK
360 370 380 390 400
VNILYTAPTA IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE
410 420 430 440 450
TVGQSRCPIV DTWWQTETGG ILISPLPGAT TLKPGSATRP MFGVVPGLVD
460 470 480 490 500
NLGNLLEGPA EGNLVILDSW PGQMRTIYKD HDRFVDTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA KVAEAAAVGV
560 570 580 590 600
PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP
610 620 630 640 650
GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK

R
Length:651
Mass (Da):71,716
Last modified:September 5, 2012 - v1
Checksum:iD85BB766C8B3B657
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1.
RefSeqiWP_014820603.1. NC_018028.1.

Genome annotation databases

EnsemblBacteriaiAFM33669; AFM33669; A458_12170.
GeneIDi13145759.
KEGGipsc:A458_12170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1.
RefSeqiWP_014820603.1. NC_018028.1.

3D structure databases

ProteinModelPortaliI4CUB2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFM33669; AFM33669; A458_12170.
GeneIDi13145759.
KEGGipsc:A458_12170.

Phylogenomic databases

KOiK01895.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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...

Entry informationi

Entry nameiI4CUB2_PSEST
AccessioniPrimary (citable) accession number: I4CUB2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: November 2, 2016
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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 one 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.