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Q12X88

- Q12X88_METBU

UniProt

Q12X88 - Q12X88_METBU

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei309 – 3091Coenzyme AUniRule annotation
Binding sitei499 – 4991ATPUniRule annotation
Binding sitei514 – 5141ATPUniRule annotation
Binding sitei522 – 5221Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei525 – 5251ATPUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi385 – 3873ATPUniRule annotation
Nucleotide bindingi409 – 4146ATPUniRule annotation

GO - Molecular functioni

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

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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi259564.Mbur_0999.

Structurei

3D structure databases

ProteinModelPortaliQ12X88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MTETIESLLK EQQEFHPSAD FVKQANMNDP HIYEKAEADI EGFWEGLAGN
60 70 80 90 100
IDWFKKWDTV LDWQPPHAKW FSGGKLNASY NCLDRHVQKH GDKPALIWEG
110 120 130 140 150
EMENSETYTY KELRDATARF AAGLKELGVK KGDVVTIYLP MVPEAVISML
160 170 180 190 200
ACSRIGAPHS VVFAGFSSEA LAQRVEDAHS RFVITCNGYF HKGNLIQQKE
210 220 230 240 250
RADKGLENAP AVEKVIVVDH AANIIPMKEE RDIWWNDLIH NVDSECEPEH
260 270 280 290 300
MDSEDTLFIM YTSGTTGRPK GVVHTTGGYM VGTNVTSNWI FDLKDDDIFW
310 320 330 340 350
CTADVGWITG HSYLVYGPLS NGATIVMHEG APDYPDKGRF WDIVEKYGVT
360 370 380 390 400
IFYTAPTAIR TFMKWGDEIP AKYDLSSLRL LGSVGEPINP KAWLWYYETI
410 420 430 440 450
GKSKCPIVDT WWQTETGMIM ISPLPGITTM RPGTATRPFP GIKANILDDE
460 470 480 490 500
GNEVPMGSGG YLALQNPWPS MIRTINGDEQ RFIDTYWSKW GADTYLTGDG
510 520 530 540 550
ARKDEDGNFW ILGRLDDVIK VSGHRLGTME IESALVSHPS VAEAAVDGKV
560 570 580 590 600
DEIKGEVICA YVILESSCDD QCSILEDELK QHVVDEIGPI ARPKMIIFTE
610 620 630 640
ELPKTRSGKI MRRVLKAITN GTEIGDISTL QDPAVVEDLK RKVNEIGEQ
Length:649
Mass (Da):72,668
Last modified:August 22, 2006 - v1
Checksum:i4C72352FF0A22D0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE51938.1.
RefSeqiYP_565688.1. NC_007955.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE51938.1 .
RefSeqi YP_565688.1. NC_007955.1.

3D structure databases

ProteinModelPortali Q12X88.
ModBasei Search...
MobiDBi 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-MImported.

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: November 26, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3