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Name5-phosphohydroxy-L-lysine phospho-lyase
Synonyms
  • 4.2.3.134
  • AGXT2L2
  • Alanine--glyoxylate aminotransferase 2-like 2
Gene NamePHYKPL
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004246|5-phosphohydroxy-L-lysine phospho-lyase
MAADQRPKADTLALRQRLISSSCRLFFPEDPVKIVRAQGQYMYDEQGAEYIDCISNVAHV
GHCHPLVVQAAHEQNQVLNTNSRYLHDNIVDYAQRLSETLPEQLCVFYFLNSGSEANDLA
LRLARHYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLDGQKEWVHVAPLPDTYRGPYRE
DHPNPAMAYANEVKRVVSSAQEKGRKIAAFFAESLPSVGGQIIPPAGYFSQVAEHIRKAG
GVFVADEIQVGFGRVGKHFWAFQLQGKDFVPDIVTMGKSIGNGHPVACVAATQPVARAFE
ATGVEYFNTFGGSPVSCAVGLAVLNVLEKEQLQDHATSVGSFLMQLLGQQKIKHPIVGDV
RGVGLFIGVDLIKDEATRTPATEEAAYLVSRLKENYVLLSTDGPGRNILKFKPPMCFSLD
NARQVVAKLDAILTDMEEKVRSCETLRLQP
Number of residues450
Molecular Weight49710.245
Theoretical pI6.76
GO Classification
Functions
  • transaminase activity
  • identical protein binding
  • lyase activity
  • pyridoxal phosphate binding
Processes
  • cellular nitrogen compound metabolic process
  • small molecule metabolic process
  • collagen catabolic process
  • extracellular matrix disassembly
  • extracellular matrix organization
  • lysine catabolic process
Components
  • mitochondrial matrix
General FunctionTransaminase activity
Specific FunctionCatalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID18027842
UniProtKB IDQ8IUZ5
UniProtKB Entry NameAT2L2_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0020593|5-phosphohydroxy-L-lysine phospho-lyase (PHYKPL)
ATGTACGATGAACAGGGGGCAGAATACATCGATTGCATCAGCAATGTGGCGCACGTTGGG
CACTGCCACCCTCTCGTGGTCCAAGCAGCACATGAGCAGAACCAGGTGCTCAACACCAAC
AGCCGGTACCTGCATGACAACATCGTGGACTATGCGCAGAGGCTGTCAGAGACCCTGCCG
GAGCAGCTCTGTGTGTTCTATTTCCTGAATTCTGGGTCAGAAGCCAATGACCTGGCCCTG
AGGCTGGCTCGCCACTACACGGGACACCAGGACGTGGTGGTATTAGATCATGCGTATCAC
GGCCACCTGAGCTCCCTGATTGACATCAGTCCCTACAAGTTCCGCAACCTGGATGGCCAG
AAGGAGTGGGTCCACGTGGCACCTCTCCCAGACACCTACCGGGGCCCCTACCGGGAGGAC
CACCCCAACCCAGCTATGGCCTATGCCAACGAGGTGAAACGTGTGGTCAGCAGTGCACAG
GAGAAGGGCAGGAAGATTGCAGCCTTCTTCGCTGAGTCTCTGCCCAGTGTGGGAGGGCAG
ATCATTCCCCCTGCTGGCTACTTCTCCCAAGTGGCAGAGCACATCCGCAAGGCCGGAGGG
GTCTTTGTTGCAGATGAGATCCAGGTTGGCTTTGGCCGGGTAGGCAAGCACTTCTGGGCC
TTCCAGCTCCAGGGAAAAGACTTCGTCCCTGACATCGTCACCATGGGCAAGTCCATTGGC
AACGGCCACCCTGTTGCCTGCGTGGCCGCAACCCAGCCTGTGGCGAGGGCATTTGAAGCC
ACCGGCGTTGAGTACTTCAACACGTTTGGGGGCAGCCCAGTGTCCTGCGCTGTGGGGCTG
GCCGTCCTGAATGTCTTGGAGAAGGAGCAGCTCCAGGATCATGCCACCAGTGTAGGCAGC
TTCCTGATGCAGCTCCTCGGGCAGCAAAAAATCAAACATCCCATCGTCGGGGATGTCAGG
GGTGTTGGGCTCTTCATTGGTGTGGATCTGATCAAAGATGAGGCCACAAGGACACCAGCA
ACTGAAGAGGCTGCCTACTTGGTATCAAGGCTGAAGGAGAACTACGTTTTGCTGAGCACT
GATGGCCCTGGGAGGAACATCCTGAAGTTTAAGCCCCCAATGTGCTTCAGCCTGGACAAT
GCACGGCAGGTGGTGGCAAAGCTGGATGCCATTCTGACTGACATGGAAGAGAAGGTGAGA
AGTTGTGAAACGCTGAGGCTCCAGCCCTAA
GenBank Gene IDAF318375
GeneCard IDNot Available
GenAtlas IDAGXT2L2
HGNC IDHGNC:28249
Chromosome Location5
Locus5q35.3
References
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  5. Veiga-da-Cunha M, Hadi F, Balligand T, Stroobant V, Van Schaftingen E: Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J Biol Chem. 2012 Mar 2;287(10):7246-55. doi: 10.1074/jbc.M111.323485. Epub 2012 Jan 12. 22241472
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