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G2MBN6 (G2MBN6_HELPX) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123
ORF Names:HPSNT_02160 EMBL AEN16601.1
OrganismHelicobacter pylori SNT49 [Complete proteome] EMBL AEN16601.1
Taxonomic identifier1055530 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region417 – 4226Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5271 By similarity HAMAP-Rule MF_01123
Metal binding5491Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5521Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3931Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5101Substrate By similarity HAMAP-Rule MF_01123
Binding site5251Substrate By similarity HAMAP-Rule MF_01123
Binding site5331Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5361Substrate By similarity HAMAP-Rule MF_01123
Binding site5981Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6231N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
G2MBN6 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: CA8F414A35DC6297

FASTA66275,016
        10         20         30         40         50         60 
MQLDDDLEFA KKVFNPNKAF AKQARIKNMC EYKDLVHEAN EDYEHFWGEL ATQKLTWFKP 

        70         80         90        100        110        120 
FDKVLNNDNA PFFKWFENGK INVSYNCIDR HLKDKKNKVA IIFEGEMGDY NVITYRKLHS 

       130        140        150        160        170        180 
EVNKTANLLK NEFNVKKGDR VIIYMPMIVE SVYMMLACAR IGAIHSIVFA GFSPEALRDR 

       190        200        210        220        230        240 
INDTQAKLVI TADGTFRKGK PYMLKPALDK ALENNACPSV EKALIVIRNA KEIDYVRGRD 

       250        260        270        280        290        300 
FVYNEMVNYQ SDKCEPEMID SEDPLFLLYT SGSTGKPKGV QHSSAGYLLW AQMTMEWVFD 

       310        320        330        340        350        360 
IRDNDNFWCT ADIGWITGHT YVVYGPLACG ATTLILEGTM SYPDYGRWWR MIEEYRVDKF 

       370        380        390        400        410        420 
YTSPTAIRML HAKGENEPLK YNLDSLKVLG TVGEPINPTA WKWFYEKIGN SKCSIVDTWW 

       430        440        450        460        470        480 
QTETGGHIIS PLPGATPIRT SCATLPLPGI HAEVLNEDGT KTKPGEQGFL CITKPWPSMI 

       490        500        510        520        530        540 
RNIWGDEKRY IDSYFSQIKL NGEYVYLSGD GAIVDENGYI TIIGRTDDIV NVSGHRIGTA 

       550        560        570        580        590        600 
EVESAISKHE MVVECAVVGI PDTIKGEGLF AFVVLCDGAK CNLGESLELL KEMNHILSIE 

       610        620        630        640        650        660 
IGKIAKLDNV MYVPGLPKTR SGKIMRRLLK SIAKKEPITQ DLSTLEDVNV VKEIMSIVQM 


EE 

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References

[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: Santal49 EMBL AEN16601.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002983 Genomic DNA. Translation: AEN16601.1.
RefSeqYP_005786582.1. NC_017376.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN16601; AEN16601; HPSNT_02160.
GeneID12366847.
KEGGhen:HPSNT_02160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycHPYL1055530:GLER-417-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2MBN6_HELPX
AccessionPrimary (citable) accession number: G2MBN6
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: February 19, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)