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Identification
HMDB Protein ID HMDBP00546
Secondary Accession Numbers
  • 5817
Name Biotinidase
Synonyms
  1. Biotinase
Gene Name BTD
Protein Type Enzyme
Biological Properties
General Function Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Specific Function Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.
Pathways
  • Biotin metabolism
  • Biotin Metabolism
  • Biotinidase Deficiency
  • Multiple carboxylase deficiency, neonatal or early onset form
  • Vitamin digestion and absorption
Reactions
Biotin amide + Water → Biotin + Ammonia details
Biocytin + Water → Biotin + L-Lysine details
GO Classification
Biological Process
nitrogen compound metabolic process
central nervous system development
epidermis development
Cellular Component
apical part of cell
nucleolus
perikaryon
extracellular space
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Molecular Function
biotinidase activity
biotin carboxylase activity
Process
metabolic process
nitrogen compound metabolic process
Cellular Location
  1. Secreted
  2. extracellular space
Gene Properties
Chromosome Location 3
Locus 3p25
SNPs BTD
Gene Sequence
>1632 bp
ATGGCGCATGCGCATATTCAGGGCGGAAGGCGCGCTAAGAGCAGATTTGTGGTCTGCATT
ATGTCTGGAGCCAGAAGTAAGCTTGCTCTTTTCCTCTGCGGCTGTTACGTGGTTGCCCTG
GGAGCCCACACCGGGGAGGAGAGCGTGGCTGACCATCACGAGGCTGAATATTATGTGGCT
GCCGTGTATGAGCATCCATCCATCCTGAGTCTGAACCCTCTGGCTCTCATCAGCCGCCAA
GAGGCCTTGGAGCTCATGAACCAGAACCTTGACATCTATGAACAGCAAGTGATGACTGCA
GCCCAAAAGGATGTACAGATTATAGTGTTTCCAGAAGATGGCATTCATGGATTCAACTTT
ACAAGAACATCCATTTATCCATTTTTGGACTTCATGCCGTCTCCCCAGGTGGTCAGGTGG
AACCCATGCCTGGAGCCTCACCGCTTCAATGACACAGAGGTGCTCCAGCGCCTGAGTTGT
ATGGCCATCAGGGGAGATATGTTCTTGGTGGCCAATCTTGGGACAAAGGAGCCTTGTCAT
AGCAGTGACCCAAGGTGCCCAAAAGATGGGAGATACCAGTTCAACACAAATGTCGTGTTC
AGCAATAATGGAACCCTTGTTGACCGCTACCGTAAACACAACCTCTACTTTGAGGCAGCA
TTCGATGTTCCTCTTAAAGTGGATCTCATCACCTTTGATACCCCCTTTGCTGGCAGGTTT
GGCATCTTCACATGCTTTGATATATTGTTCTTTGACCCTGCCATCAGAGTCCTCAGAGAC
TACAAGGTGAAGCATGTTGTGTACCCAACTGCCTGGATGAACCAGCTCCCACTCTTGGCA
GCAATTGAGATTCAGAAAGCTTTTGCTGTTGCCTTTGGCATCAACGTTCTGGCAGCTAAT
GTCCACCACCCAGTTCTGGGGATGACAGGAAGTGGCATACACACCCCTCTGGAGTCCTTT
TGGTACCATGACATGGAAAATCCCAAAAGTCACCTTATAATTGCCCAGGTGGCCAAAAAT
CCAGTGGGTCTCATTGGTGCAGAGAATGCAACAGGTGAAACGGACCCATCCCATAGTAAG
TTTTTAAAAATTTTGTCAGGCGATCCGTACTGTGAGAAGGATGCTCAGGAAGTCCACTGT
GATGAGGCCACCAAGTGGAACGTGAATGCTCCTCCCACATTTCACTCTGAGATGATGTAT
GACAATTTCACCCTGGTCCCTGTCTGGGGAAAGGAAGGCTATCTCCACGTCTGTTCCAAT
GGCCTCTGCTGTTATTTACTTTACGAGAGGCCCACCTTATCCAAAGAGCTGTATGCCCTG
GGGGTCTTTGATGGGCTTCACACAGTACATGGCACTTACTACATCCAAGTGTGTGCCCTG
GTCAGGTGTGGGGGTCTTGGCTTCGACACCTGTGGACAGGAAATCACAGAGGCCACGGGG
ATATTTGAGTTTCACCTGTGGGGCAACTTCAGTACTTCCTATATCTTTCCTTTGTTTCTG
ACCTCAGGGATGACCCTAGAAGTCCCTGACCAGCTTGGCTGGGAGAATGACCACTATTTC
CTGAGGAAAAGTAGGCTGTCCTCTGGGCTGGTGACGGCGGCTCTCTATGGGCGCTTGTAT
GAGAGGGACTAG
Protein Properties
Number of Residues 543
Molecular Weight 61132.43
Theoretical pI 6.254
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Biotinidase
MAHAHIQGGRRAKSRFVVCIMSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVA
AVYEHPSILSLNPLALISRQEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNF
TRTSIYPFLDFMPSPQVVRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCH
SSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRF
GIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN
VHHPVLGMTGSGIHTPLESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSK
FLKILSGDPYCEKDAQEVHCDEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSN
GLCCYLLYERPTLSKELYALGVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATG
IFEFHLWGNFSTSYIFPLFLTSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLY
ERD
GenBank ID Protein 4557373
UniProtKB/Swiss-Prot ID P43251
UniProtKB/Swiss-Prot Entry Name BTD_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_000060.2
GeneCard ID BTD
GenAtlas ID BTD
HGNC ID HGNC:1122
References
General References
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  4. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
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  6. Cole H, Reynolds TR, Lockyer JM, Buck GA, Denson T, Spence JE, Hymes J, Wolf B: Human serum biotinidase. cDNA cloning, sequence, and characterization. J Biol Chem. 1994 Mar 4;269(9):6566-70. [PubMed:7509806 ]
  7. Knight HC, Reynolds TR, Meyers GA, Pomponio RJ, Buck GA, Wolf B: Structure of the human biotinidase gene. Mamm Genome. 1998 Apr;9(4):327-30. [PubMed:9530634 ]
  8. Pomponio RJ, Norrgard KJ, Hymes J, Reynolds TR, Buck GA, Baumgartner R, Suormala T, Wolf B: Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of profound biotinidase deficiency in symptomatic children. Hum Genet. 1997 Apr;99(4):506-12. [PubMed:9099842 ]
  9. Swango KL, Demirkol M, Huner G, Pronicka E, Sykut-Cegielska J, Schulze A, Mayatepek E, Wolf B: Partial biotinidase deficiency is usually due to the D444H mutation in the biotinidase gene. Hum Genet. 1998 May;102(5):571-5. [PubMed:9654207 ]
  10. Norrgard KJ, Pomponio RJ, Swango KL, Hymes J, Reynolds T, Buck GA, Wolf B: Double mutation (A171T and D444H) is a common cause of profound biotinidase deficiency in children ascertained by newborn screening the the United States. Mutations in brief no. 128. Online. Hum Mutat. 1998;11(5):410. [PubMed:10206677 ]