SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A9IIL7

- A9IIL7_BORPD

UniProt

A9IIL7 - A9IIL7_BORPD

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Bpet1782
Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei318 – 3181Coenzyme A By similarityUniRule annotation
Binding sitei398 – 3981Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei512 – 5121Substrate By similarityUniRule annotation
Binding sitei527 – 5271Substrate By similarityUniRule annotation
Active sitei529 – 5291 By similarityUniRule annotation
Binding sitei535 – 5351Coenzyme A By similarityUniRule annotation
Binding sitei538 – 5381Substrate By similarityUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi551 – 5511Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi554 – 5541Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei599 – 5991Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

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 annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciBPET340100:GJBO-1806-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:Bpet1782Imported
OrganismiBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Taxonomic identifieri340100 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001225: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei624 – 6241N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi340100.Bpet1782.

Structurei

3D structure databases

ProteinModelPortaliA9IIL7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni422 – 4276Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiGGCEAVT.
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.

A9IIL7-1 [UniParc]FASTAAdd to Basket

« Hide

MSNTIESVLV ETRVFPPPER AAQGARIGSM DAYRALCQEV EQDFDGFWTR    50
QARENLTWSK PFTQVLDESN APFYRWFGDG ELNVSANCLD VHLNNGNADK 100
TAIIFESDDG KVDKVTYREL LARVCRFANG LKSLGYKKGD RAIIYMPMSI 150
QAVVAMQACA RLGVTHSVVF GGFSAKSLQE RIVDVGASLV ITADEQVRGG 200
KTIPLKPAVE EAIGMGGCDA VTKIVVYKRT GGNVPWQDGR DLWMHDVEAG 250
QPDTCEPVPV NAEHPLFILY TSGSTGKPKG VQHSSGGYLL WALLTVKWTF 300
DARPDDVYWC TADVGWVTGH TYITYGPLAA GLTQIVFEGV PTYPDAGRFW 350
DMIARHKVTT FYTAPTAIRS LIKASEATPA AHPRNYDLNS LRIIGTVGEP 400
INPEAWVWYH KNVGQERCPI VDTWWQTETG GHMINPLPGA TPTKPGSCTL 450
PLPGIAATVV DETGAEVEPG NGGFLAIKRP WPAMIRTIWG DPERFKKSYF 500
PPELRGYYLA GDGAQRDADG YFWIMGRIDD VLNVSGHRLG TMEVESALVS 550
HELVAEAAVV GRPDDTTGEA VVAFVVLKRA RPEGDEAQAI AKQLRDWVGK 600
EIGPIAKPKD IRFGDNLPKT RSGKIMRRLL RVVAKGEQIT QDVSTLENPA 650
ILDQLAKSV 659
Length:659
Mass (Da):72,328
Last modified:February 5, 2008 - v1
Checksum:iB9F6B19C56639FE2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM902716 Genomic DNA. Translation: CAP42121.1.
RefSeqiWP_012248704.1. NC_010170.1.
YP_001630390.1. NC_010170.1.

Genome annotation databases

EnsemblBacteriaiCAP42121; CAP42121; Bpet1782.
GeneIDi5821098.
KEGGibpt:Bpet1782.
PATRICi21165015. VBIBorPet31633_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM902716 Genomic DNA. Translation: CAP42121.1 .
RefSeqi WP_012248704.1. NC_010170.1.
YP_001630390.1. NC_010170.1.

3D structure databases

ProteinModelPortali A9IIL7.
ModBasei Search...

Protein-protein interaction databases

STRINGi 340100.Bpet1782.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP42121 ; CAP42121 ; Bpet1782 .
GeneIDi 5821098.
KEGGi bpt:Bpet1782.
PATRICi 21165015. VBIBorPet31633_1772.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi GGCEAVT.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci BPET340100:GJBO-1806-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

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: September 3, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi