GenomeNet

Database: UniProt
Entry: A0A2U9C984_SCOMX
LinkDB: A0A2U9C984_SCOMX
Original site: A0A2U9C984_SCOMX 
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
//
DBGET integrated database retrieval system