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D7BFC2

- D7BFC2_MEISD

UniProt

D7BFC2 - D7BFC2_MEISD

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161Coenzyme AUniRule annotation
Binding sitei340 – 3401Coenzyme AUniRule annotation
Binding sitei506 – 5061ATPUniRule annotation
Binding sitei521 – 5211ATPUniRule annotation
Binding sitei529 – 5291Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei532 – 5321ATPUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi548 – 5481Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi392 – 3943ATPUniRule annotation
Nucleotide bindingi416 – 4216ATPUniRule 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 annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD7BFC2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2014Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQSADRIEA VLKEERVFYP SEDFKRSALL AKPEEYQALY EESLRDPEGF
60 70 80 90 100
WGRFAGEFHW FEPWKKVLEW NVPYAKWFVG GKTNLTYNAL DRHLASRRNK
110 120 130 140 150
AAIVFEGEPG DSRVLTYHDL HREVSKFANV LKGLGVNKGD RVTIYLPMIP
160 170 180 190 200
EAAIAMLACA RIGAIHSVVF GGFSASALAE RINDAQSAVL VTADGGWRRG
210 220 230 240 250
SVVPLKANAD EALASTESVR HVVVVRRVGQ EVPMLPGRDH WYHELMASAS
260 270 280 290 300
DRCEAEPLDS EHPLFILYTS GSTGKPKGVM HTTAGYMAYV ALTARYVFDL
310 320 330 340 350
KETDTYFCTA DVGWVTGHSY VVYGLLLNGA TTLMYEGAPN WPDEGRIWNI
360 370 380 390 400
IDKYGVSILY TAPTAIRAFM KWGEQWPLKY RLSSLRLLGS VGEPINPEAW
410 420 430 440 450
LWYYHVIGKG RCPIVDTWWQ TETGGIMITT LPGVHPMKPG HAGKPFFGVE
460 470 480 490 500
PDIVDTSGKT ITGADEGGHL IIKRPWPSML RTVWGDPERY ERQYWSQYPG
510 520 530 540 550
NYFTGDGARR DSDGYYLIMG RVDDVLNVSG HRLGTMEVES ALVSHPAVAE
560 570 580 590 600
AAVVGRPDPI KGEGIVAFVT LKAGYTPSDA LSAELKAHVV KAIGAIARPD
610 620 630 640 650
EIRFTEAMPK TRSGKIMRRL LRQIAAGESE IKGDTSTLED RSVVERLKAA

Q
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.
RefSeqiYP_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 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-R2Imported.

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: October 29, 2014
This is version 27 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