(data stored in SCRATCH zone)

SWISSPROT: A8FPL6_SHESH

ID   A8FPL6_SHESH            Unreviewed;       264 AA.
AC   A8FPL6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00646000};
DE            EC=3.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00645997};
DE   AltName: Full=Biotin synthesis protein BioH {ECO:0000256|HAMAP-Rule:MF_01260};
DE   AltName: Full=Carboxylesterase BioH {ECO:0000256|HAMAP-Rule:MF_01260};
GN   Name=bioH {ECO:0000256|HAMAP-Rule:MF_01260};
GN   OrderedLocusNames=Ssed_0176 {ECO:0000313|EMBL:ABV34789.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34789.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34789.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34789.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The physiological role of BioH is to remove the methyl
CC       group introduced by BioC when the pimeloyl moiety is complete. It
CC       allows to synthesize pimeloyl-ACP via the fatty acid synthetic
CC       pathway through the hydrolysis of the ester bonds of pimeloyl-ACP
CC       esters. {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00645987}.
CC   -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] methyl ester +
CC       H(2)O = pimeloyl-[acyl-carrier protein] + methanol.
CC       {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00646002}.
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00645991}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00645993}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00646004}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       Carboxylesterase BioH family. {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00645995}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01260}.
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DR   EMBL; CP000821; ABV34789.1; -; Genomic_DNA.
DR   RefSeq; WP_012004315.1; NC_009831.1.
DR   ProteinModelPortal; A8FPL6; -.
DR   STRING; 425104.Ssed_0176; -.
DR   ESTHER; shesh-a8fpl6; BioH.
DR   EnsemblBacteria; ABV34789; ABV34789; Ssed_0176.
DR   KEGG; sse:Ssed_0176; -.
DR   eggNOG; ENOG4105D3C; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000028062; -.
DR   KO; K02170; -.
DR   OMA; LHGWGMN; -.
DR   OrthoDB; POG091H04D0; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01260; Carboxylester; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010076; BioH.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01738; bioH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPL6.
DR   SWISS-2DPAGE; A8FPL6.
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00645985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00645998};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00645988, ECO:0000313|EMBL:ABV34789.1};
KW   Serine esterase {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00645990}.
FT   DOMAIN       17    222       AB hydrolase-1 (Alpha/Beta hydrolase fold
FT                                1). {ECO:0000259|Pfam:PF00561}.
FT   REGION       81     82       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01260}.
FT   ACT_SITE     81     81       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
FT   ACT_SITE    208    208       {ECO:0000256|HAMAP-Rule:MF_01260}.
FT   ACT_SITE    236    236       {ECO:0000256|HAMAP-Rule:MF_01260}.
FT   BINDING      23     23       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
FT   BINDING     236    236       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
SQ   SEQUENCE   264 AA;  29644 MW;  445ECA463F23D49B CRC64;
     MNPSPLHIES IGQGQEIIIL HGWGVNSAVF TPLHSSLSQY RVHYVDLPGF GHSSMIEGDI
     DAWVDAITSR LSHKAIWVGW SLGGLVATRA ALRYPERVQG LVTIASSPCF MAREEESWPG
     IPPQVLSDFS KQLGSDLSKT IDRFLAIQAM GSVTAKDDIK QLRELVLSRP LPETTALVQG
     LDMLKSVDLR PQIAQIEQPW LRIWGRLDGL IPRRVPPLMP KDEQLYQDLI LHRASHAPFI
     SHRDEFITGL VSWIEKLVRD ELLR
//

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