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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Status
Reviewed-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 sitei308Coenzyme AUniRule annotation1
Binding sitei332Coenzyme AUniRule annotation1
Binding sitei497ATPUniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei520Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei523ATPUniRule annotation1
Metal bindingi534Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi536Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei581Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi384 – 386ATPUniRule annotation3
Nucleotide bindingi408 – 413ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, 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
Ordered Locus Names:Plav_1331
OrganismiParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Taxonomic identifieri402881 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhodobiaceaeParvibaculum
Proteomesi
  • UP000006377 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000730441 – 647Acetyl-coenzyme A synthetaseAdd BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei606N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi402881.Plav_1331.

Structurei

3D structure databases

ProteinModelPortaliA7HSR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 193Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
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.

A7HSR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEIFPVPA EWKKRAIVDA EKYRHMYEAS INDPESFWRR EGLRIDWMKP
60 70 80 90 100
YTKIKDTSFD PHNVSIKWFE DGTLNASVNC IDRHLERRAG QVAIIWEGDD
110 120 130 140 150
PSIDRKITYR ELHDEVCRFA NVLKARGVKK GDRVTIYMPM IPEAAYAMLA
160 170 180 190 200
CARIGAVHSV VFGGFSPDSL AGRIVDCASS CVITADEGVR GGRKIPLKAN
210 220 230 240 250
TDEALKKCPG VKSVIVVKHT GGAVAMEKGR DVWYAEEAAK VSATCAPEEM
260 270 280 290 300
NAEDPLFILY TSGSTGKPKG VLHTTGGYMV YASMTHQYVF DYHDGDIYWC
310 320 330 340 350
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPDASRCW QVIDKHEVNI
360 370 380 390 400
FYTAPTALRA LMREGEEPVK KTSRKSLRLL GSVGEPINPE AWLWYHRVVG
410 420 430 440 450
DGRCPIVDTW WQTETGGILI SPLPGAIATK PGSATKPFFG VQPVIVDAEG
460 470 480 490 500
NVQEGATTGN LCIDDSWPGQ MRTVYGDHQR FVETYFIQYP GRYFTGDGCR
510 520 530 540 550
RDEDGYYWIT GRVDDVLNVS GHRMGTAEVE SALVAHPKVA EAAVVGYPHD
560 570 580 590 600
IKGQGIYAYV TLIAGEAATE ELRKELVTWV RKEIGPIASP DLIQFAPGLP
610 620 630 640
KTRSGKIMRR ILRKIAEDDF SNLGDTSTLA DPSVVTDLVD NRQNKAG
Length:647
Mass (Da):71,661
Last modified:September 11, 2007 - v1
Checksum:i43419A3302E5FBE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000774 Genomic DNA. Translation: ABS62951.1.
RefSeqiWP_012110225.1. NC_009719.1.

Genome annotation databases

EnsemblBacteriaiABS62951; ABS62951; Plav_1331.
KEGGipla:Plav_1331.
PATRICi22864268. VBIParLav90819_1372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000774 Genomic DNA. Translation: ABS62951.1.
RefSeqiWP_012110225.1. NC_009719.1.

3D structure databases

ProteinModelPortaliA7HSR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi402881.Plav_1331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS62951; ABS62951; Plav_1331.
KEGGipla:Plav_1331.
PATRICi22864268. VBIParLav90819_1372.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
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 nameiACSA_PARL1
AccessioniPrimary (citable) accession number: A7HSR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 11, 2007
Last modified: November 2, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.