ID   BIOHC_TERTT             Reviewed;         570 AA.
AC   C5BMZ8;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Biotin biosynthesis bifunctional protein BioHC;
DE   Includes:
DE     RecName: Full=Carboxylesterase BioH;
DE              EC=3.1.1.1;
DE     AltName: Full=Biotin synthesis protein BioH;
DE   Includes:
DE     RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase;
DE              Short=Malonyl-ACP O-methyltransferase;
DE              EC=2.1.1.197;
DE     AltName: Full=Biotin synthesis protein BioC;
GN   Name=bioC; OrderedLocusNames=TERTU_0492;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
CC   -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester to
CC       its methyl ester by transfer of a methyl group from S-adenosyl-L-
CC       methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty
CC       acid synthetic pathway (By similarity). {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl
CC         ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17105, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9954, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78845; EC=2.1.1.197;
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AB hydrolase
CC       superfamily. Carboxylesterase BioH family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the methyltransferase
CC       superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001614; ACR11632.1; -; Genomic_DNA.
DR   RefSeq; WP_015817744.1; NC_012997.1.
DR   AlphaFoldDB; C5BMZ8; -.
DR   SMR; C5BMZ8; -.
DR   STRING; 377629.TERTU_0492; -.
DR   ESTHER; tertt-c5bmz8; BioH.
DR   PRIDE; C5BMZ8; -.
DR   EnsemblBacteria; ACR11632; ACR11632; TERTU_0492.
DR   KEGG; ttu:TERTU_0492; -.
DR   eggNOG; COG0596; Bacteria.
DR   eggNOG; COG2021; Bacteria.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_550729_0_0_6; -.
DR   OMA; AHTINEG; -.
DR   OrthoDB; 1664438at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000009080; Chromosome.
DR   GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00835; BioC; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR011814; BioC.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR02072; BioC; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Hydrolase; Methyltransferase; Multifunctional enzyme;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..570
FT                   /note="Biotin biosynthesis bifunctional protein BioHC"
FT                   /id="PRO_0000413326"
FT   REGION          1..279
FT                   /note="Carboxylesterase"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..570
FT                   /note="Malonyl-ACP O-methyltransferase"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   570 AA;  63934 MW;  6B0D342802532F76 CRC64;
     MTEVNVRAAA TPEEKPFLNR TRHEPANPQP NRSVLVFLHG WGSDKRQWQS FVPTLLEALG
     DEREMVFIDL PGFGDNSDFR CDDLEHMLKQ LARIIPGNAT LIGWSLGGMI ATQLASRHPE
     KIGRLITIAT NPLFVKNDAE IAAGKAPWKH AMERETFSDF VNGFADDPEA TLKRFIALQS
     MGDSERRQVT DTLKNLLSFS AHSQQTCWAN ALSYLDQLDN RTALRNLTQP ALHIYGKSDA
     LVPVRAGRAL QGLAPSHWVE SITAAGHAPH ISHPREVATM INSFLRQQAP RLSQRKRRIA
     NSFSSAAQEY DTLARLQKRV VDSLVEFSLG TGGSVGQTLL DLGCGTGYCI ERLLQQFPEI
     TQPEGRIHAL DIAEGMLDRA QQKFDELGVA EQINWHLGDM ESLPFVDESF DGCISSLTVQ
     WSENPLQLFS EMYRALKPGG WFALSTLGPE TLFELRSAWR MVDEFAHVNK FLSLESVKSV
     AEQAGLQMVA YKSETPVLYY HSVVHLMREL KGIGAHTINE GRQNGLMGRA TFRRLEEAYD
     NWLDPDRGLP ARYEVYYIYL RKPLDESASA