ID   FUMD_SPHMC              Reviewed;         540 AA.
AC   D2D3B6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Fumonisin B1 esterase;
DE            EC=3.1.1.87;
GN   Name=fumD;
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=MTA144;
RX   PubMed=19922747; DOI=10.1016/j.jbiotec.2009.11.004;
RA   Heinl S., Hartinger D., Thamhesl M., Vekiru E., Krska R., Schatzmayr G.,
RA   Moll W.-D., Grabherr R.;
RT   "Degradation of fumonisin B1 by the consecutive action of two bacterial
RT   enzymes.";
RL   J. Biotechnol. 145:120-129(2010).
CC   -!- FUNCTION: Involved in degradation of fumonisin B1. Catalyzes the
CC       hydrolysis of fumonisin B1 (FB1) to aminopentol (HFB1).
CC       {ECO:0000269|PubMed:19922747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fumonisin B1 + 2 H2O = (2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-
CC         12,16-dimethylicosane-3,5,10,14,15-pentol + 2 H(+) + 2
CC         tricarballylate; Xref=Rhea:RHEA:30363, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:62517, ChEBI:CHEBI:62526,
CC         ChEBI:CHEBI:62554; EC=3.1.1.87;
CC         Evidence={ECO:0000269|PubMed:19922747};
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ426269; ACS27056.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2D3B6; -.
DR   SMR; D2D3B6; -.
DR   ESTHER; sphmc-FumD; Carb_B_Bacteria.
DR   KEGG; ag:ACS27056; -.
DR   BioCyc; MetaCyc:MON-16400; -.
DR   BRENDA; 3.1.1.87; 8963.
DR   GO; GO:0004104; F:cholinesterase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..540
FT                   /note="Fumonisin B1 esterase"
FT                   /id="PRO_0000418896"
FT   REGION          521..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        240
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        356
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        448
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  57362 MW;  5BD31149760AC53E CRC64;
     MKEHQCRGGR ASPAAPATWL ARISVSRGAS AIAWTFMLGA TAIPVAAQTD DPKLVRHTQS
     GAVEGVEGDV ETFLGIPFAA PPVGDLRWRP PAPPRAWAGT RDGRRFAPDC IGNERLREGS
     RAAGTSEDCL YLNIWSPKQV GKGGLPVMIW VYGGGFSGGS GAVPYYDGSA LAQKGVVVVT
     FNYRAGILGF LAHPALSKES PNGVSGNYGL LDMLAAFKWV QNNIREFGGD PNRVTVFGES
     AGASALGLLL TSPLSESAFN QAILQSPGLA RPLATLSESE ANGLELGADI SALRRADAGE
     LTKIAQSRIP MSRQFTKPRP MGPILDGYVL RTLDVDAFAK GAFRKIPVLV GGNADEGRAF
     TDRLPVKTVL EYRAYLTEQF GDEADAWERC YPANSDADVP AAVARLFGDS QFNNGIELLS
     AAFAKWRTPL WRYRFTGIPG AGRRPATHGD EIPYVFANLG PSSVSMFGSL EGGAGASDIK
     LATEMSAAWV SFAVHGVPDQ GTKSHWPRFE RRGEIMTFGS QVGSGEGLGV SPSKACQPSK