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Q30QK3

- Q30QK3_SULDN

UniProt

Q30QK3 - Q30QK3_SULDN

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Suden_1451
Organism
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))
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 sitei307 – 3071Coenzyme A By similarityUniRule annotation
Binding sitei383 – 3831Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei500 – 5001Substrate By similarityUniRule annotation
Binding sitei515 – 5151Substrate By similarityUniRule annotation
Active sitei517 – 5171 By similarityUniRule annotation
Binding sitei523 – 5231Coenzyme A By similarityUniRule annotation
Binding sitei526 – 5261Substrate By similarityUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei586 – 5861Coenzyme 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

BioCyciSDEN326298:GH9P-1500-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:Suden_1451Imported
OrganismiSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))Imported
Taxonomic identifieri326298 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas
ProteomesiUP000002714: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-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

STRINGi326298.Suden_1451.

Structurei

3D structure databases

ProteinModelPortaliQ30QK3.

Family & Domainsi

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.

Q30QK3-1 [UniParc]FASTAAdd to Basket

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MNREVFKPNK EFSKSARIKN MCEYQDLQEY ALEDYEGFWG SYAKEKLEWM    50
QPFTNVMNES NFPFVKWFEG GKLNVSVQCI DRHLKSRKNK AAIIFEGDRG 100
DKQIITYLEL YYNVNKFANL LKNEFDVKKG DRVIIYMPMI PEAAYAMLAC 150
ARIGAIHSIV FGGFSAEALK DRVIDAGAKV VITADGAYRK DKPYMLKPVV 200
DEALRGETPV KKVLVVERNG EDVTWVAGRD YSYNELIKHQ SGKCEPEVMD 250
SEDPLFLLYT SGSTGKPKGV QHNSAGYILW AQMTMEWVFD VKENDTYWCT 300
ADVGWITGHT YIVYGPLAMG ATTIMFEGVP TYPDAGRPWK MVEEYKVNQF 350
YTAPTAIRVL HKTGENEPAK YDLSSLKVLG TVGEPIDPPA WKWYYEAIGG 400
SKCAIVDTYW QTETGGHIVS PLPGATPIKP ACATFPLPGI MAEILDENGN 450
RAEVGEKGLM CVTRPWPAMI RGVWGDEERF VKSYFGDVKK DGKPVYFTGD 500
GAIYDEDGYI TITGRTDDVI NVSGHRMGTA EVEAAIKKHP NVAEVAVVGK 550
PHEIKGEGIF AYIVLKSDSG IADEVEEVKA INKVIQKEIG NIALCDDVVF 600
VVGLPKTRSG KIMRRILRSI AKGEEITQDI STLEDPSIVA TIASAVQSCR 650
L 651
Length:651
Mass (Da):72,616
Last modified:December 6, 2005 - v1
Checksum:i7A53E3EDCBB4CCC8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000153 Genomic DNA. Translation: ABB44728.1.
RefSeqiYP_393963.1. NC_007575.1.

Genome annotation databases

EnsemblBacteriaiABB44728; ABB44728; Suden_1451.
GeneIDi3763349.
KEGGitdn:Suden_1451.
PATRICi23771544. VBISulDen68967_1506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000153 Genomic DNA. Translation: ABB44728.1 .
RefSeqi YP_393963.1. NC_007575.1.

3D structure databases

ProteinModelPortali Q30QK3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 326298.Suden_1451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB44728 ; ABB44728 ; Suden_1451 .
GeneIDi 3763349.
KEGGi tdn:Suden_1451.
PATRICi 23771544. VBISulDen68967_1506.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SDEN326298:GH9P-1500-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 33889 / DSM 1251.

Entry informationi

Entry nameiQ30QK3_SULDN
AccessioniPrimary (citable) accession number: Q30QK3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 62 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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