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Q12X88

- Q12X88_METBU

UniProt

Q12X88 - Q12X88_METBU

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Mbur_0999
Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
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 sitei309 – 3091Coenzyme A By similarityUniRule annotation
Binding sitei385 – 3851Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei499 – 4991Substrate By similarityUniRule annotation
Binding sitei514 – 5141Substrate By similarityUniRule annotation
Active sitei516 – 5161 By similarityUniRule annotation
Binding sitei522 – 5221Coenzyme A By similarityUniRule annotation
Binding sitei525 – 5251Substrate By similarityUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei584 – 5841Coenzyme 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 annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciMBUR259564:GHBZ-1022-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:Mbur_0999Imported
OrganismiMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)Imported
Taxonomic identifieri259564 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides
ProteomesiUP000001979: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-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

STRINGi259564.Mbur_0999.

Structurei

3D structure databases

ProteinModelPortaliQ12X88.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 4146Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiQTAILFE.

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.

Q12X88-1 [UniParc]FASTAAdd to Basket

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MTETIESLLK EQQEFHPSAD FVKQANMNDP HIYEKAEADI EGFWEGLAGN    50
IDWFKKWDTV LDWQPPHAKW FSGGKLNASY NCLDRHVQKH GDKPALIWEG 100
EMENSETYTY KELRDATARF AAGLKELGVK KGDVVTIYLP MVPEAVISML 150
ACSRIGAPHS VVFAGFSSEA LAQRVEDAHS RFVITCNGYF HKGNLIQQKE 200
RADKGLENAP AVEKVIVVDH AANIIPMKEE RDIWWNDLIH NVDSECEPEH 250
MDSEDTLFIM YTSGTTGRPK GVVHTTGGYM VGTNVTSNWI FDLKDDDIFW 300
CTADVGWITG HSYLVYGPLS NGATIVMHEG APDYPDKGRF WDIVEKYGVT 350
IFYTAPTAIR TFMKWGDEIP AKYDLSSLRL LGSVGEPINP KAWLWYYETI 400
GKSKCPIVDT WWQTETGMIM ISPLPGITTM RPGTATRPFP GIKANILDDE 450
GNEVPMGSGG YLALQNPWPS MIRTINGDEQ RFIDTYWSKW GADTYLTGDG 500
ARKDEDGNFW ILGRLDDVIK VSGHRLGTME IESALVSHPS VAEAAVDGKV 550
DEIKGEVICA YVILESSCDD QCSILEDELK QHVVDEIGPI ARPKMIIFTE 600
ELPKTRSGKI MRRVLKAITN GTEIGDISTL QDPAVVEDLK RKVNEIGEQ 649
Length:649
Mass (Da):72,668
Last modified:August 22, 2006 - v1
Checksum:i4C72352FF0A22D0B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000300 Genomic DNA. Translation: ABE51938.1.
RefSeqiWP_011499087.1. NC_007955.1.
YP_565688.1. NC_007955.1.

Genome annotation databases

EnsemblBacteriaiABE51938; ABE51938; Mbur_0999.
GeneIDi3998104.
KEGGimbu:Mbur_0999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000300 Genomic DNA. Translation: ABE51938.1 .
RefSeqi WP_011499087.1. NC_007955.1.
YP_565688.1. NC_007955.1.

3D structure databases

ProteinModelPortali Q12X88.
ModBasei Search...

Protein-protein interaction databases

STRINGi 259564.Mbur_0999.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE51938 ; ABE51938 ; Mbur_0999 .
GeneIDi 3998104.
KEGGi mbu:Mbur_0999.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi QTAILFE.

Enzyme and pathway databases

BioCyci MBUR259564:GHBZ-1022-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: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Entry informationi

Entry nameiQ12X88_METBU
AccessioniPrimary (citable) accession number: Q12X88
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: September 3, 2014
This is version 55 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

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