ID A0A2K6C095_MACNE Unreviewed; 428 AA.
AC A0A2K6C095;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=5-phosphohydroxy-L-lysine phospho-lyase {ECO:0000313|Ensembl:ENSMNEP00000017058.1};
GN Name=PHYKPL {ECO:0000313|Ensembl:ENSMNEP00000017058.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000017058.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000017058.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR AlphaFoldDB; A0A2K6C095; -.
DR STRING; 9545.ENSMNEP00000017058; -.
DR Ensembl; ENSMNET00000041283.1; ENSMNEP00000017058.1; ENSMNEG00000032543.1.
DR GeneTree; ENSGT00940000159222; -.
DR OMA; FWGWQAH; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032543; Expressed in lymph node and 12 other cell types or tissues.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; -; 1.
DR PANTHER; PTHR45688:SF6; 5-PHOSPHOHYDROXY-L-LYSINE PHOSPHO-LYASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
SQ SEQUENCE 428 AA; 47245 MW; F58399F2AA98FEE5 CRC64;
MAADRRSKAD TLALRQRLIS SSCRLFFPED PVKIVRAQGQ YMYDEQGAEY IDCINNVAHG
QYHTSGWQAS LKGNPGVHRK SGRRISSRKP CPRNILFFFF LDSSSEANDL ALRLARHYTG
HQDVVVLDHA YHGHLSSLID ISPYKFRNLD GQKEWVHVAP LPDTYRGPYR EDHPNPAVAY
ANEVKRVVSS AQEKGRKIAA FFAESLPSVG GQIIPPAGYF SQVAEHIHKA GGVFVADEIQ
VGFGRVGKHF WAFQLQGKDF VPDIVTMGKS IGNGHPVACV ATTQPVARAF EATGVEYFNT
FGGSPVSCAV GLAVLNVLEK EQLQAHATSV GSFLMELLRG VGLFIGVDLI KDEATRTPAT
EEAAYLVSRL KENYVLLSTD GPGRNILKFK PPMCFSLDNA RQVVAKLDAI LTDMEEKVRS
CQTLRLQL
//