(data stored in ACNUC7421 zone)

SWISSPROT: BIOH_AERHH

ID   BIOH_AERHH              Reviewed;         254 AA.
AC   A0KF11;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 88.
DE   RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000255|HAMAP-Rule:MF_01260};
DE            EC=3.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01260};
DE   AltName: Full=Biotin synthesis protein BioH {ECO:0000255|HAMAP-Rule:MF_01260};
DE   AltName: Full=Carboxylesterase BioH {ECO:0000255|HAMAP-Rule:MF_01260};
GN   Name=bioH {ECO:0000255|HAMAP-Rule:MF_01260}; OrderedLocusNames=AHA_0299;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: The physiological role of BioH is to remove the methyl group
CC       introduced by BioC when the pimeloyl moiety is complete. It allows to
CC       synthesize pimeloyl-ACP via the fatty acid synthetic pathway through
CC       the hydrolysis of the ester bonds of pimeloyl-ACP esters.
CC       {ECO:0000255|HAMAP-Rule:MF_01260}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + pimeloyl-[ACP] methyl ester = H(+) + methanol +
CC         pimeloyl-[ACP]; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, Rhea:RHEA-
CC         COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; EC=3.1.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01260};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01260}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01260}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC       BioH family. {ECO:0000255|HAMAP-Rule:MF_01260}.
DR   EMBL; CP000462; ABK36065.1; -; Genomic_DNA.
DR   RefSeq; WP_011704304.1; NC_008570.1.
DR   RefSeq; YP_854829.1; NC_008570.1.
DR   SMR; A0KF11; -.
DR   STRING; 380703.AHA_0299; -.
DR   ESTHER; aerhh-a0kf11; BioH.
DR   EnsemblBacteria; ABK36065; ABK36065; AHA_0299.
DR   GeneID; 4488758; -.
DR   KEGG; aha:AHA_0299; -.
DR   PATRIC; fig|380703.7.peg.287; -.
DR   eggNOG; ENOG4105D3C; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000028062; -.
DR   KO; K02170; -.
DR   OMA; LHGWGMN; -.
DR   BioCyc; AHYD380703:G1G7B-300-MONOMER; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
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   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01738; bioH; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KF11.
DR   SWISS-2DPAGE; A0KF11.
KW   Biotin biosynthesis; Cytoplasm; Hydrolase; Reference proteome;
KW   Serine esterase.
FT   CHAIN           1..254
FT                   /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT                   esterase"
FT                   /id="PRO_1000214122"
FT   DOMAIN          14..242
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          82..83
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   REGION          143..147
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         20
FT                   /note="Substrate; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         235
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ   SEQUENCE   254 AA;  27945 MW;  3B91FFC7D1D7A603 CRC64;
     MSVSVERFGQ GPDLVLLHGW GMNGAVWHGI VPALASRYRV HLVDLPGFGN SPLAGEVEYS
     LPWLAEEVAA ILPEQCHLLG WSLGGLVASQ LALSHPERLH SLITVASSPC FMARDEWPGI
     APKVLAGFNQ MLAGDFKQTI ERFLAIQAMG SEHARDDIRQ LRHWLAERPA PQLAALEAGL
     GLLAEVDLRD ELTPLSLPWL RVYGRLDSLV PKASIPLLDE RYPSSRSVVL EKASHAPFIS
     HPQQFIEIIE HFVG
//

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