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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pantoea sp. (strain At-9b)
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
Ordered Locus Names:Pat9b_0328Imported
OrganismiPantoea sp. (strain At-9b)Imported
Taxonomic identifieri592316 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaePantoea
Proteomesi
  • UP000001624 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

Interactioni

Protein-protein interaction databases

STRINGi592316.Pat9b_0328.

Structurei

3D structure databases

ProteinModelPortaliE6WHR8.
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

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.
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.

E6WHR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQIHKHPVP AAIAENALIN AEQYAAMYQQ SVDDPETFWG EQGKILDWIT
60 70 80 90 100
PYSKVKNTSF APGNVAIRWY EDGTLNLAAN CLDRHLASRG DHPAIIWEGD
110 120 130 140 150
DANESKTLTF RQLHADVCRF ANVLGSLGVK KGDVVAIYMP MVPEAAIAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSNA KLVITADEGI RAGRGIPLKK
210 220 230 240 250
NVDDALNNPN VTSVKNVVVF KRTGKDTGWR EGRDLWWHDL MADAADQHQP
260 270 280 290 300
VAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDV
310 320 330 340 350
YWCTADVGWV TGHSYLIYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHK
360 370 380 390 400
VTLLYTAPTA IRALMAEGDK AIEGTDRSSL RIMGSVGEPI NPEAWEWYYN
410 420 430 440 450
KIGDGRCPIV DTWWQTETGG FMITPLPGAI ELKAGSATKP FFGVQPALVD
460 470 480 490 500
NEGNTLEGAT EGNLVIVDSW PGQARTLFGD HDRFEQTYFS TFKNRYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI
560 570 580 590 600
PHSIKGQAIY AYITLNHGEE PSPELYTEVR NWVRKEIGPI ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVEK LLEEKQSIKM

P
Length:651
Mass (Da):71,523
Last modified:March 8, 2011 - v1
Checksum:iF10BEEDD2003560E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002433 Genomic DNA. Translation: ADU67654.1.
RefSeqiWP_013507523.1. NC_014837.1.

Genome annotation databases

EnsemblBacteriaiADU67654; ADU67654; Pat9b_0328.
KEGGipao:Pat9b_0328.
PATRICi45314927. VBIPanSp129740_0326.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002433 Genomic DNA. Translation: ADU67654.1.
RefSeqiWP_013507523.1. NC_014837.1.

3D structure databases

ProteinModelPortaliE6WHR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi592316.Pat9b_0328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADU67654; ADU67654; Pat9b_0328.
KEGGipao:Pat9b_0328.
PATRICi45314927. VBIPanSp129740_0326.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.
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 nameiE6WHR8_PANSA
AccessioniPrimary (citable) accession number: E6WHR8
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: November 30, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.