ID   F7ED31_CALJA            Unreviewed;       532 AA.
AC   F7ED31;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Biotinidase {ECO:0000256|ARBA:ARBA00039680};
DE            EC=3.5.1.12 {ECO:0000256|ARBA:ARBA00039012};
GN   Name=BTD {ECO:0000313|Ensembl:ENSCJAP00000006356.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000006356.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000006356.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000006356.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalytic release of biotin from biocytin, the product of
CC       biotin-dependent carboxylases degradation.
CC       {ECO:0000256|ARBA:ARBA00037073}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=biocytin + H2O = biotin + L-lysine; Xref=Rhea:RHEA:77171,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:57586,
CC         ChEBI:CHEBI:195545; EC=3.5.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00043697};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000256|ARBA:ARBA00008225}.
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DR   RefSeq; XP_002759736.2; XM_002759690.4.
DR   AlphaFoldDB; F7ED31; -.
DR   Ensembl; ENSCJAT00000006709.4; ENSCJAP00000006356.4; ENSCJAG00000003498.5.
DR   GeneID; 100409568; -.
DR   KEGG; cjc:100409568; -.
DR   CTD; 686; -.
DR   GeneTree; ENSGT00390000013823; -.
DR   InParanoid; F7ED31; -.
DR   Proteomes; UP000008225; Chromosome 17.
DR   Bgee; ENSCJAG00000003498; Expressed in liver and 6 other cell types or tissues.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07567; biotinidase_like; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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:SF14; BIOTINIDASE; 1.
DR   PANTHER; PTHR10609; BIOTINIDASE-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF19018; Vanin_C; 1.
DR   PIRSF; PIRSF011861; Biotinidase; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..532
FT                   /note="Biotinidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035268917"
FT   DOMAIN          61..340
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   COILED          65..92
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        101
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011861-1"
SQ   SEQUENCE   532 AA;  59784 MW;  C0BF13ABEFBCF1F3 CRC64;
     MPSRFMVCIM SGTRSKLALF LCGCYVVALG AHTGEECVAR HHEAESYVAA VYEHPSILSP
     NPLALTSRQQ ALELMNQNLD IYEQQVMTAA QKGVQIMVFP EDGIHGFNFT RTSIYPFLDF
     MPSPQVVRWN PCLEPHRFND TEVLQRLSCM AIKGDMFLVA NLGTKQPCHI NDPGCPDDGR
     YQFNTDVVFS SNGTLVDRYR KHNLYFEAAF DVPLQVDHTT FDTPFAGRFG VFTCFDILFF
     SPAVRLLRDY EVKHVVYPTA WMNQLPLLAA IEIQKAFAVA FGVNVLAANV HHPVLGMTGS
     GIHTPLKSFW YHDMENPNGR LIIAQVAKNP VGLIDAENAT GEMDPSHSKF LKILSGDPYC
     EKDAQEVHCD EATKWNRNAL PIFHSEMMYD NFTLVPVWGK EGYLHVCSNG LCCYLLYERP
     TVSEELYALG VFDGLHTVHG TYYIQVCALV RCGGLGFDTC GQEITEATGI FEFHLWGNFS
     TSYIFPLFLT SGMTLDVPDQ LGWENDHYFL RKSGLSSGLV TAALYGRLYE RD
//