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Protein

Pimeloyl-[acyl-carrier protein] methyl ester esterase

Gene

bioH

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Pimeloyl-[acyl-carrier protein] methyl ester + H2O = pimeloyl-[acyl-carrier protein] + methanol.UniRule annotation

Pathwayi: biotin biosynthesis

This protein is involved in the pathway biotin biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei22Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1
Active sitei82NucleophileUniRule annotation1
Active sitei207UniRule annotation1
Active sitei235UniRule annotation1
Binding sitei235SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Serine esterase
Biological processBiotin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00078

Protein family/group databases

ESTHERishifl-BIOH BioH

Names & Taxonomyi

Protein namesi
Recommended name:
Pimeloyl-[acyl-carrier protein] methyl ester esteraseUniRule annotation (EC:3.1.1.85UniRule annotation)
Alternative name(s):
Biotin synthesis protein BioHUniRule annotation
Carboxylesterase BioHUniRule annotation
Gene namesi
Name:bioHUniRule annotation
Ordered Locus Names:SF3435, S4329
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002044941 – 262Pimeloyl-[acyl-carrier protein] methyl ester esteraseAdd BLAST262

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Beta strandi13 – 19Combined sources7
Helixi26 – 31Combined sources6
Helixi33 – 37Combined sources5
Beta strandi40 – 45Combined sources6
Helixi61 – 69Combined sources9
Beta strandi74 – 81Combined sources8
Helixi83 – 94Combined sources12
Helixi96 – 98Combined sources3
Beta strandi99 – 106Combined sources8
Helixi122 – 133Combined sources12
Helixi136 – 148Combined sources13
Helixi154 – 167Combined sources14
Helixi173 – 185Combined sources13
Helixi191 – 194Combined sources4
Beta strandi199 – 204Combined sources6
Beta strandi208 – 210Combined sources3
Helixi214 – 221Combined sources8
Beta strandi225 – 230Combined sources6
Helixi237 – 240Combined sources4
Helixi242 – 256Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ETWX-ray2.05A/C1-257[»]
ProteinModelPortaliQ83PW0
SMRiQ83PW0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 242AB hydrolase-1Sequence analysisAdd BLAST228

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 83Substrate bindingUniRule annotation2
Regioni143 – 147Substrate bindingUniRule annotation5

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D3C Bacteria
COG0596 LUCA
HOGENOMiHOG000028062
KOiK02170
OMAiLHGWGMN

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
HAMAPiMF_01260 Carboxylester, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
IPR010076 BioH
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR01738 bioH, 1 hit

Sequencei

Sequence statusi: Complete.

Q83PW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNIWWQTKG QGNVHLVLLH GWGLNAEVWR CIDEELSSHF TLHLVDLPGF
60 70 80 90 100
GRSRGFGALS LADMAEAVLQ QAPDKAIWLG WSLGGLVASQ IALTHPERVQ
110 120 130 140 150
ALVTVASSPC FSARDEWPGI KPDVLAGFQQ QLSDDFQRTV ERFLALQTMG
160 170 180 190 200
TETARQDARA LKKTVLALPM PEVDVLNGGL EILKTVDLRQ PLQNVSMPFL
210 220 230 240 250
RLYGYLDGLV PRKVVPMLDK LWPHSESYIF AKAAHAPFIS HPVEFCHLLV
260
ALKQRVLVVS ES
Length:262
Mass (Da):29,148
Last modified:July 5, 2005 - v4
Checksum:i468108F08E5C0312
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA Translation: AAN44896.2
AE014073 Genomic DNA Translation: AAP19285.1
RefSeqiNP_709189.2, NC_004337.2
WP_001060072.1, NZ_MTPK01000074.1

Genome annotation databases

EnsemblBacteriaiAAN44896; AAN44896; SF3435
AAP19285; AAP19285; S4329
GeneIDi1026527
KEGGisfl:SF3435
sfx:S4329
PATRICifig|198214.7.peg.4052

Similar proteinsi

Entry informationi

Entry nameiBIOH_SHIFL
AccessioniPrimary (citable) accession number: Q83PW0
Secondary accession number(s): Q7UAT4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2005
Last modified: April 25, 2018
This is version 101 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health