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G2MBN6

- G2MBN6_HELPX

UniProt

G2MBN6 - G2MBN6_HELPX

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, HPSNT_02160
Organism
Helicobacter pylori SNT49
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 sitei317 – 3171Coenzyme A By similarityUniRule annotation
Binding sitei393 – 3931Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei510 – 5101Substrate By similarityUniRule annotation
Binding sitei525 – 5251Substrate By similarityUniRule annotation
Active sitei527 – 5271 By similarityUniRule annotation
Binding sitei533 – 5331Coenzyme A By similarityUniRule annotation
Binding sitei536 – 5361Substrate By similarityUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi552 – 5521Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei598 – 5981Coenzyme A By similarityUniRule 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

BioCyciHPYL1055530:GLER-417-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
ORF Names:HPSNT_02160Imported
OrganismiHelicobacter pylori SNT49Imported
Taxonomic identifieri1055530 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000008534: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei623 – 6231N6-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

ProteinModelPortaliG2MBN6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni417 – 4226Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.

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.

G2MBN6-1 [UniParc]FASTAAdd to Basket

« Hide

MQLDDDLEFA KKVFNPNKAF AKQARIKNMC EYKDLVHEAN EDYEHFWGEL    50
ATQKLTWFKP FDKVLNNDNA PFFKWFENGK INVSYNCIDR HLKDKKNKVA 100
IIFEGEMGDY NVITYRKLHS EVNKTANLLK NEFNVKKGDR VIIYMPMIVE 150
SVYMMLACAR IGAIHSIVFA GFSPEALRDR INDTQAKLVI TADGTFRKGK 200
PYMLKPALDK ALENNACPSV EKALIVIRNA KEIDYVRGRD FVYNEMVNYQ 250
SDKCEPEMID SEDPLFLLYT SGSTGKPKGV QHSSAGYLLW AQMTMEWVFD 300
IRDNDNFWCT ADIGWITGHT YVVYGPLACG ATTLILEGTM SYPDYGRWWR 350
MIEEYRVDKF YTSPTAIRML HAKGENEPLK YNLDSLKVLG TVGEPINPTA 400
WKWFYEKIGN SKCSIVDTWW QTETGGHIIS PLPGATPIRT SCATLPLPGI 450
HAEVLNEDGT KTKPGEQGFL CITKPWPSMI RNIWGDEKRY IDSYFSQIKL 500
NGEYVYLSGD GAIVDENGYI TIIGRTDDIV NVSGHRIGTA EVESAISKHE 550
MVVECAVVGI PDTIKGEGLF AFVVLCDGAK CNLGESLELL KEMNHILSIE 600
IGKIAKLDNV MYVPGLPKTR SGKIMRRLLK SIAKKEPITQ DLSTLEDVNV 650
VKEIMSIVQM EE 662
Length:662
Mass (Da):75,016
Last modified:November 16, 2011 - v1
Checksum:iCA8F414A35DC6297
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002983 Genomic DNA. Translation: AEN16601.1.
RefSeqiYP_005786582.1. NC_017376.1.

Genome annotation databases

EnsemblBacteriaiAEN16601; AEN16601; HPSNT_02160.
GeneIDi12366847.
KEGGihen:HPSNT_02160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002983 Genomic DNA. Translation: AEN16601.1 .
RefSeqi YP_005786582.1. NC_017376.1.

3D structure databases

ProteinModelPortali G2MBN6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEN16601 ; AEN16601 ; HPSNT_02160 .
GeneIDi 12366847.
KEGGi hen:HPSNT_02160.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci HPYL1055530:GLER-417-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. Kersulyte D., Choudhury A., Mukhopadhyay A.K., Nair G.B., Berg D.E.
    Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Santal49Imported.

Entry informationi

Entry nameiG2MBN6_HELPX
AccessioniPrimary (citable) accession number: G2MBN6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: June 11, 2014
This is version 16 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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