ID K7EV64_PONAB Unreviewed; 545 AA. AC K7EV64; A0A2J8U3X6; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 24-JUL-2024, entry version 55. DE RecName: Full=Biotinidase {ECO:0000256|ARBA:ARBA00039680}; DE EC=3.5.1.12 {ECO:0000256|ARBA:ARBA00039012}; GN Name=BTD {ECO:0000313|Ensembl:ENSPPYP00000024444.2}; GN ORFNames=CR201_G0030559 {ECO:0000313|EMBL:PNJ39966.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000024444.2, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000024444.2, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PNJ39966.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ39966.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M., RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J., RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M., RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B., RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPPYP00000024444.2} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) 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}. 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; NDHI03003471; PNJ39966.1; -; Genomic_DNA. DR Ensembl; ENSPPYT00000033705.2; ENSPPYP00000024444.2; ENSPPYG00000014086.3. DR GeneTree; ENSGT00390000013823; -. DR HOGENOM; CLU_033209_0_0_1; -. DR OMA; SGKWNPC; -. DR OrthoDB; 4006627at2759; -. DR Proteomes; UP000001595; Chromosome 3. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro. DR GO; GO:0006768; P:biotin metabolic process; IEA:TreeGrafter. 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:UP000001595}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 74..353 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT COILED 78..105 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 114 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" FT ACT_SITE 214 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" FT ACT_SITE 247 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" SQ SEQUENCE 545 AA; 61562 MW; E5C55FD4AE4B1C4E CRC64; MARKETQLII KMTHLARFMV CIMSGARSKL ALFLCGCYVV ALGAHTGEES VAEHHEAEYY MAAVYEHPSI LSLNPLALVS RQEALELMNQ NLDIYEQQVM TAAQKGVQII VFPEDGIHGF NFTRTSIYPF LDFMPSPQVV RWNPCLEPHR FSDTEVLQRL SCMAIRGDMF LVANLGTKQP CHSSDPRCPK DGRYQFNTNV VFSNNGTLVD RYRKHNLYFE AAFDVPLKVD HITFDTPFAG RFGIFTCFDI LFFDPTIRLL RDYKVKHVVY PTAWMNQLPL LAAIEIQKAF AVAFGINVLA ANVHHPVLGM TGSGIHTPLE SFWYHDMENP KSHLIIAQVA KNPVGLIGAE NATGETDPSH SKFLKILSGD PYCEKDAQEV HCDEATQWNV NAPPTFHSEM MYDNFTLVPV WGKEGYLHVC SNGFCCYLLY KRPSLSKELY ALGVFNGLHT VHGTYYIQVC ALVRCGGLGF DTCGQEITEA TGIFEFHLWG NFSTSYIFPL FLTSGMTLEV PDQLGWENDH YFLRKSRLSS GLVTAALYGR LYERD //