ID   BTD_TAKRU               Reviewed;         504 AA.
AC   Q8AV84;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Biotinidase;
DE            Short=Biotinase;
DE            EC=3.5.1.12;
DE   Flags: Precursor;
GN   Name=btd;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kosan C., Kunz J.;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic release of biotin from biocytin, the product of
CC       biotin-dependent carboxylases degradation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=biotin amide + H2O = biotin + NH4(+); Xref=Rhea:RHEA:13081,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16615, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57586; EC=3.5.1.12;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {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; AF527754; AAO15005.1; -; Genomic_DNA.
DR   RefSeq; XP_011607778.1; XM_011609476.1.
DR   AlphaFoldDB; Q8AV84; -.
DR   SMR; Q8AV84; -.
DR   STRING; 31033.ENSTRUP00000037989; -.
DR   Ensembl; ENSTRUT00000038125; ENSTRUP00000037989; ENSTRUG00000014869.
DR   GeneID; 101069377; -.
DR   KEGG; tru:101069377; -.
DR   CTD; 686; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   GeneTree; ENSGT00390000013823; -.
DR   InParanoid; Q8AV84; -.
DR   Proteomes; UP000005226; Chromosome 12.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0047708; F:biotinidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07567; biotinidase_like; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR012101; Biotinidase-like_euk.
DR   InterPro; IPR040154; Biotinidase/VNN.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR043957; Vanin_C.
DR   PANTHER; PTHR10609; PTHR10609; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF19018; Vanin_C; 1.
DR   PIRSF; PIRSF011861; Biotinidase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..504
FT                   /note="Biotinidase"
FT                   /id="PRO_0000019709"
FT   DOMAIN          30..309
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        79
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   504 AA;  55552 MW;  FA719C5478AA0FE4 CRC64;
     MFSFGTVFTF ALLLIPLTEA VDSSYVAAVY EHNLILNPDP RVPLSRLEAL QHLQKNLDIF
     EVQAARAAQQ GAQIIVFPED GLHGFNFSRT SISAYLETVP DPEQESWNPC LEPLRHNNTE
     VLQQLSCMAR RNNLYLVANM ADLQPCSVSA APSSCPPDGR WQFNTNVVFR SDGLLVARYH
     KYNLYFEAAF DAPPEPEIVT FDTPFAGKFG LITCFDILFQ EPTVILVEKG VRQIIFPAAW
     MNQLPLLDII QFQRAFSLGA NVTLLAANIR NDQLIMTGSG IYTPFSATYH HAQRGDPEEG
     RLLVARVPVL DPEWLGHNAA SGEAAAVDES SGYCYSETCL DSPASTAPVF VSSMMYDPFT
     FALLNATDGE MRVCNGTFCC YLQYRWVTET GRTELYALGA FDGTHTVNGR YAVQVCALVR
     CAGSDASSCG QEVDEAESKL DFMLEGKFAS RHVYPSVLSS GMVLEQPERV EAAADGRVSL
     KHSNVMGGLV TACLYGRMHH LDTA