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Protein

Pimeloyl-[acyl-carrier protein] methyl ester esterase

Gene

bioH

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Biotin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00078.

Protein family/group databases

ESTHERishifl-BIOH. BioH.
MEROPSiS33.994.

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiQ83PW0.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF3435.

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.
OMAiLICELIS.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01260. Carboxylester. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR010076. BioH.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
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_LVJC01000074.1.

Genome annotation databases

EnsemblBacteriaiAAN44896; AAN44896; SF3435.
AAP19285; AAP19285; S4329.
GeneIDi1026527.
KEGGisfl:SF3435.
sft:NCTC1_03715.
sfx:S4329.
PATRICi18710656. VBIShiFle31049_4732.

Cross-referencesi

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_LVJC01000074.1.

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...

Protein-protein interaction databases

STRINGi198214.SF3435.

Protein family/group databases

ESTHERishifl-BIOH. BioH.
MEROPSiS33.994.

Proteomic databases

PaxDbiQ83PW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN44896; AAN44896; SF3435.
AAP19285; AAP19285; S4329.
GeneIDi1026527.
KEGGisfl:SF3435.
sft:NCTC1_03715.
sfx:S4329.
PATRICi18710656. VBIShiFle31049_4732.

Phylogenomic databases

eggNOGiENOG4105D3C. Bacteria.
COG0596. LUCA.
HOGENOMiHOG000028062.
KOiK02170.
OMAiLICELIS.

Enzyme and pathway databases

UniPathwayiUPA00078.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01260. Carboxylester. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR010076. BioH.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01738. bioH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBIOH_SHIFL
AccessioniPrimary (citable) accession number: Q83PW0
Secondary accession number(s): Q7UAT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2005
Last modified: November 2, 2016
This is version 90 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.