ID   BTD_BOVIN               Reviewed;         525 AA.
AC   A6QQ07;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Biotinidase;
DE            Short=Biotinase;
DE            EC=3.5.1.12 {ECO:0000250|UniProtKB:P43251};
DE   Flags: Precursor;
GN   Name=BTD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic release of biotin from biocytin, the product of
CC       biotin-dependent carboxylases degradation.
CC       {ECO:0000250|UniProtKB:P43251}.
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         Evidence={ECO:0000250|UniProtKB:P43251};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13082;
CC         Evidence={ECO:0000250|UniProtKB:P43251};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:P43251}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
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DR   EMBL; BC149584; AAI49585.1; -; mRNA.
DR   RefSeq; NP_001095676.1; NM_001102206.1.
DR   AlphaFoldDB; A6QQ07; -.
DR   SMR; A6QQ07; -.
DR   STRING; 9913.ENSBTAP00000025464; -.
DR   PaxDb; A6QQ07; -.
DR   PRIDE; A6QQ07; -.
DR   GeneID; 537669; -.
DR   KEGG; bta:537669; -.
DR   CTD; 686; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   InParanoid; A6QQ07; -.
DR   OrthoDB; 1276751at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0047708; F:biotinidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006768; P:biotin metabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..525
FT                   /note="Biotinidase"
FT                   /id="PRO_0000368204"
FT   DOMAIN          54..333
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   525 AA;  58353 MW;  FB119581060A5403 CRC64;
     MSRAGRQLAL LLCSCCVAVA IPGGLAEEGC PAEPHQASRY VAAVYEHQSF LSPDPLALTS
     REQALELMHR NLDVYEQQVT TAARKGAQII VFPEDGIHGF NFTRTSIYPF LDFMPSPRSV
     RWNPCLEPHR FNDTEVLQRL SCMAMKGEMF LVANLGTKQP CHSSDPGCPS DGRYQFNTNV
     VFSSNGTLVD RYRKHNLYFE AAFDTPLEVD HTVFDTPFAG KFGVFTCFDI LFFDPAVRLL
     QDSEVKHVVY PTAWMNQLPL LAAIQIQRGF AIAFVINLLA ANIHHPSLGM TGSGIHTPLK
     SFWHHSMDSP EGHLIIAEVA RNPPGLISAG NATGKTDPFH RKFLQLLAGD PYSEKDAQDV
     HCDAAPKSTT NASPTFNSEM MYDNFTLVPV WGRDGHVHVC AHGLCCHLLY QRPTVSQELY
     ALGVFDGLHT VHGTYYVQVC ALVKCGGLGF DTCGQEITEA MGMFEFHLWG NFSTSYIFPM
     LLTSGMMLET PDQLGWESDQ YFLKKRGLSS GLVTAALYGR LYERD