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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
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 sitei318Coenzyme AUniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei527ATPUniRule annotation1
Binding sitei535Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei538ATPUniRule annotation1
Metal bindingi549Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi551Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi554Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi398 – 400ATPUniRule annotation3
Nucleotide bindingi422 – 427ATPUniRule 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:Bpet1782Imported
OrganismiBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)Imported
Taxonomic identifieri340100 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000001225 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei624N6-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

STRINGi340100.Bpet1782.

Structurei

3D structure databases

ProteinModelPortaliA9IIL7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 88ACAS_NInterPro annotationAdd BLAST56
Domaini96 – 534AMP-bindingInterPro annotationAdd BLAST439
Domaini543 – 624AMP-binding_CInterPro annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni198 – 201Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiIKNMCEY.
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.

A9IIL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTIESVLV ETRVFPPPER AAQGARIGSM DAYRALCQEV EQDFDGFWTR
60 70 80 90 100
QARENLTWSK PFTQVLDESN APFYRWFGDG ELNVSANCLD VHLNNGNADK
110 120 130 140 150
TAIIFESDDG KVDKVTYREL LARVCRFANG LKSLGYKKGD RAIIYMPMSI
160 170 180 190 200
QAVVAMQACA RLGVTHSVVF GGFSAKSLQE RIVDVGASLV ITADEQVRGG
210 220 230 240 250
KTIPLKPAVE EAIGMGGCDA VTKIVVYKRT GGNVPWQDGR DLWMHDVEAG
260 270 280 290 300
QPDTCEPVPV NAEHPLFILY TSGSTGKPKG VQHSSGGYLL WALLTVKWTF
310 320 330 340 350
DARPDDVYWC TADVGWVTGH TYITYGPLAA GLTQIVFEGV PTYPDAGRFW
360 370 380 390 400
DMIARHKVTT FYTAPTAIRS LIKASEATPA AHPRNYDLNS LRIIGTVGEP
410 420 430 440 450
INPEAWVWYH KNVGQERCPI VDTWWQTETG GHMINPLPGA TPTKPGSCTL
460 470 480 490 500
PLPGIAATVV DETGAEVEPG NGGFLAIKRP WPAMIRTIWG DPERFKKSYF
510 520 530 540 550
PPELRGYYLA GDGAQRDADG YFWIMGRIDD VLNVSGHRLG TMEVESALVS
560 570 580 590 600
HELVAEAAVV GRPDDTTGEA VVAFVVLKRA RPEGDEAQAI AKQLRDWVGK
610 620 630 640 650
EIGPIAKPKD IRFGDNLPKT RSGKIMRRLL RVVAKGEQIT QDVSTLENPA

ILDQLAKSV
Length:659
Mass (Da):72,328
Last modified:February 5, 2008 - v1
Checksum:iB9F6B19C56639FE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM902716 Genomic DNA. Translation: CAP42121.1.

Genome annotation databases

EnsemblBacteriaiCAP42121; CAP42121; Bpet1782.
KEGGibpt:Bpet1782.
PATRICi21165015. VBIBorPet31633_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM902716 Genomic DNA. Translation: CAP42121.1.

3D structure databases

ProteinModelPortaliA9IIL7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi340100.Bpet1782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP42121; CAP42121; Bpet1782.
KEGGibpt:Bpet1782.
PATRICi21165015. VBIBorPet31633_1772.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiIKNMCEY.
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 nameiA9IIL7_BORPD
AccessioniPrimary (citable) accession number: A9IIL7
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: November 2, 2016
This is version 62 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.