(data stored in ACNUC1104 zone)

SWISSPROT: D3UYB8_XENBS

ID   D3UYB8_XENBS            Unreviewed;       258 AA.
AC   D3UYB8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00064125};
DE            EC=3.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00064111};
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   ECO:0000313|EMBL:CBJ79296.1};
GN   OrderedLocusNames=XBJ1_0145 {ECO:0000313|EMBL:CBJ79296.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79296.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79296.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79296.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:SAAS00186858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + pimeloyl-[ACP] methyl ester = H(+) + methanol +
CC         pimeloyl-[ACP]; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955,
CC         Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735;
CC         EC=3.1.1.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01260,
CC         ECO:0000256|SAAS:SAAS01122655};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00064128}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00064113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00064118}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       Carboxylesterase BioH family. {ECO:0000256|HAMAP-Rule:MF_01260,
CC       ECO:0000256|SAAS:SAAS00561353}.
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DR   EMBL; FN667741; CBJ79296.1; -; Genomic_DNA.
DR   RefSeq; WP_012986763.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0145; -.
DR   ESTHER; xenbs-d3uyb8; BioH.
DR   EnsemblBacteria; CBJ79296; CBJ79296; XBJ1_0145.
DR   GeneID; 8829769; -.
DR   KEGG; xbo:XBJ1_0145; -.
DR   PATRIC; fig|406818.4.peg.132; -.
DR   eggNOG; ENOG4105D3C; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000028062; -.
DR   KO; K02170; -.
DR   OMA; LHGWGMN; -.
DR   BioCyc; XBOV406818:XBJ1_RS00645-MONOMER; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002045; 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   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01738; bioH; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYB8.
DR   SWISS-2DPAGE; D3UYB8.
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00448363};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00448366};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00448354, ECO:0000313|EMBL:CBJ79296.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Serine esterase {ECO:0000256|HAMAP-Rule:MF_01260,
KW   ECO:0000256|SAAS:SAAS00448359}.
FT   DOMAIN       16    241       AB hydrolase-1. {ECO:0000259|Pfam:
FT                                PF00561}.
FT   REGION       82     83       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01260}.
FT   REGION      143    147       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01260}.
FT   ACT_SITE     82     82       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
FT   ACT_SITE    207    207       {ECO:0000256|HAMAP-Rule:MF_01260}.
FT   ACT_SITE    235    235       {ECO:0000256|HAMAP-Rule:MF_01260}.
FT   BINDING      22     22       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
FT   BINDING     235    235       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01260}.
SQ   SEQUENCE   258 AA;  28800 MW;  AC9986F8C1351C85 CRC64;
     MNKLFWQIMG EAPRDLVMLH GWGLNSEVWR SVETRLSSHF RLHLVDLPGH GRSQPYPAMT
     LAEMADTVWQ QAPENALWLG WSLGGLVASR IALDHPAEVA GLITVASSPK FSAEGDWPGI
     KPTVLRAFEH QLSEDFQKTV ERFLSLQTLG TDSARQDARL LKSVILNQPM PTVEVLNAGL
     ETLRTDDLRA ELAQLQLPFL RLYGYLDGLV PRKIAAQLDN EWPHTHSVIM RNAAHAPFVS
     HPDEFVDAVM EFVANAGL
//

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