ID A0A2U9C984_SCOMX Unreviewed; 334 AA.
AC A0A2U9C984;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 9.
DE SubName: Full=Putative 5-phosphohydroxy-L-lysine phospho-lyase isoform 3 {ECO:0000313|EMBL:AWP12179.1};
GN ORFNames=SMAX5B_008821 {ECO:0000313|EMBL:AWP12179.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP12179.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP12179.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP026255; AWP12179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9C984; -.
DR Proteomes; UP000246464; Chromosome 13.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 1.
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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AWP12179.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
SQ SEQUENCE 334 AA; 37286 MW; 6A165B1F8F4478C2 CRC64;
MALRTLGKEE TLAMRSRLIG QSCRLFYSDD PVKIVRARGQ YLYDENNQRY LDCISNVHHV
GHCHPSITKA AAAQMDLLNT NTRFLHDNIV VYAERLAAAL PEKLGVFYFV NSGSEANDLA
LRLAQQYTQH KDVIVLDHAY HGHLMSLIDI SPYKFRKLAG QKDWVHVAPL PDTYRGKYRE
DHPNPGQAYA DTVKDLIGEV HMKGRKICAF FAESLPSVGG QIVLPRGYSA KVAEYVRSAG
GVFVADEVQT GFGRVGSHFW GFQLQGEDFC PDIVTLGKPM GNGHPLACVA TTAEIAGAFT
ANSVEYFNTT SRPRTLNWKR KTSKVFSANL WYIS
//