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A8A5M0 (BIOH_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pimeloyl-[acyl-carrier protein] methyl ester esterase

EC=3.1.1.85
Alternative name(s):
Biotin synthesis protein BioH
Carboxylesterase BioH
Gene names
Name:bioH
Ordered Locus Names:EcHS_A3609
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters By similarity. HAMAP-Rule MF_01260

Catalytic activity

Pimeloyl-[acyl-carrier protein] methyl ester + H2O = pimeloyl-[acyl-carrier protein] + methanol. HAMAP-Rule MF_01260

Pathway

Cofactor biosynthesis; biotin biosynthesis. HAMAP-Rule MF_01260

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01260

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01260.

Sequence similarities

Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family.

Ontologies

Keywords
   Biological processBiotin biosynthesis
   Cellular componentCytoplasm
   Molecular functionHydrolase
Serine esterase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processbiotin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarboxylic ester hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Pimeloyl-[acyl-carrier protein] methyl ester esterase HAMAP-Rule MF_01260
PRO_1000067265

Regions

Region82 – 832Substrate binding By similarity
Region143 – 1475Substrate binding By similarity

Sites

Active site821Nucleophile By similarity
Active site2071 By similarity
Active site2351 By similarity
Binding site221Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site2351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A5M0 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 931226F241A940F3

FASTA25628,533
        10         20         30         40         50         60 
MNNIWWQTKG QGNVHLVLLH GWGLNAEVWR CIDEELSSHF TLHLVDLPGF GRSRGFGALS 

        70         80         90        100        110        120 
LADMAEAVLQ QAPDKAIWLG WSLGGLVASQ IALTHPERVQ ALVTVASSPC FSARDEWPGI 

       130        140        150        160        170        180 
KPDVLAGFQQ QLSDDFQRTV ERFLALQTMG TETARQDARA LKKTVLALPM PEVDVLNGGL 

       190        200        210        220        230        240 
EILKTVDLRQ PLQNVSMPFL RLYGYLDGLV PRKVVPMLDK LWPHSESYIF AKAAHAPFIS 

       250 
HPVEFCHLLV ALKQRV 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV07824.1.
RefSeqYP_001460207.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A5M0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A3609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV07824; ABV07824; EcHS_A3609.
GeneID5594704.
KEGGecx:EcHS_A3609.
PATRIC18317174. VBIEscCol77814_3515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0596.
HOGENOMHOG000028062.
KOK02170.
OMALICELIS.
OrthoDBEOG6FJNH9.
ProtClustDBPRK10349.

Enzyme and pathway databases

BioCycECOL331112:GHHI-3605-MONOMER.
UniPathwayUPA00078.

Family and domain databases

HAMAPMF_01260. Carboxylester.
InterProIPR010076. BioH.
[Graphical view]
TIGRFAMsTIGR01738. bioH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOH_ECOHS
AccessionPrimary (citable) accession number: A8A5M0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways