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D7BFC2

- D7BFC2_MEISD

UniProt

D7BFC2 - D7BFC2_MEISD

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Mesil_1588
Organism
Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus)
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 annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161Coenzyme A By similarityUniRule annotation
Binding sitei340 – 3401Coenzyme A By similarityUniRule annotation
Binding sitei392 – 3921Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei506 – 5061Substrate By similarityUniRule annotation
Binding sitei521 – 5211Substrate By similarityUniRule annotation
Active sitei523 – 5231 By similarityUniRule annotation
Binding sitei529 – 5291Coenzyme A By similarityUniRule annotation
Binding sitei532 – 5321Substrate By similarityUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi548 – 5481Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei590 – 5901Coenzyme 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

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

BioCyciMSIL526227:GJ9Q-1617-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:Mesil_1588Imported
OrganismiMeiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus)Imported
Taxonomic identifieri526227 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus
ProteomesiUP000001916: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei615 – 6151N6-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

Structurei

3D structure databases

ProteinModelPortaliD7BFC2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni416 – 4216Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

D7BFC2-1 [UniParc]FASTAAdd to Basket

« Hide

MDQSADRIEA VLKEERVFYP SEDFKRSALL AKPEEYQALY EESLRDPEGF    50
WGRFAGEFHW FEPWKKVLEW NVPYAKWFVG GKTNLTYNAL DRHLASRRNK 100
AAIVFEGEPG DSRVLTYHDL HREVSKFANV LKGLGVNKGD RVTIYLPMIP 150
EAAIAMLACA RIGAIHSVVF GGFSASALAE RINDAQSAVL VTADGGWRRG 200
SVVPLKANAD EALASTESVR HVVVVRRVGQ EVPMLPGRDH WYHELMASAS 250
DRCEAEPLDS EHPLFILYTS GSTGKPKGVM HTTAGYMAYV ALTARYVFDL 300
KETDTYFCTA DVGWVTGHSY VVYGLLLNGA TTLMYEGAPN WPDEGRIWNI 350
IDKYGVSILY TAPTAIRAFM KWGEQWPLKY RLSSLRLLGS VGEPINPEAW 400
LWYYHVIGKG RCPIVDTWWQ TETGGIMITT LPGVHPMKPG HAGKPFFGVE 450
PDIVDTSGKT ITGADEGGHL IIKRPWPSML RTVWGDPERY ERQYWSQYPG 500
NYFTGDGARR DSDGYYLIMG RVDDVLNVSG HRLGTMEVES ALVSHPAVAE 550
AAVVGRPDPI KGEGIVAFVT LKAGYTPSDA LSAELKAHVV KAIGAIARPD 600
EIRFTEAMPK TRSGKIMRRL LRQIAAGESE IKGDTSTLED RSVVERLKAA 650
Q 651
Length:651
Mass (Da):72,374
Last modified:August 10, 2010 - v1
Checksum:iD8E7C2C5D25B4AF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002042 Genomic DNA. Translation: ADH63475.1.
RefSeqiWP_013158039.1. NC_014212.1.
YP_003684983.1. NC_014212.1.

Genome annotation databases

EnsemblBacteriaiADH63475; ADH63475; Mesil_1588.
GeneIDi9251092.
KEGGimsv:Mesil_1588.
PATRICi38191955. VBIMeiSil18825_1623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002042 Genomic DNA. Translation: ADH63475.1 .
RefSeqi WP_013158039.1. NC_014212.1.
YP_003684983.1. NC_014212.1.

3D structure databases

ProteinModelPortali D7BFC2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADH63475 ; ADH63475 ; Mesil_1588 .
GeneIDi 9251092.
KEGGi msv:Mesil_1588.
PATRICi 38191955. VBIMeiSil18825_1623.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci MSIL526227:GJ9Q-1617-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 700542 / DSM 9946 / VI-R2.

Entry informationi

Entry nameiD7BFC2_MEISD
AccessioniPrimary (citable) accession number: D7BFC2
Entry historyi
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: September 3, 2014
This is version 25 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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