ID A0A2U9CQ37_SCOMX Unreviewed; 785 AA.
AC A0A2U9CQ37;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative pyridoxal-dependent decarboxylase domain-containing protein 1 {ECO:0000313|EMBL:AWP18283.1};
GN ORFNames=SMAX5B_004410 {ECO:0000313|EMBL:AWP18283.1};
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:AWP18283.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18283.1, 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};
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DR EMBL; CP026261; AWP18283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CQ37; -.
DR STRING; 52904.ENSSMAP00000024263; -.
DR Proteomes; UP000246464; Chromosome 19.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF1; PYRIDOXAL-DEPENDENT DECARBOXYLASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT REGION 667..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 86536 MW; 66F0C2FC490825FC CRC64;
MVDSTLAQVG KNLSEAMMIL GDGQREMEMG TERRRFSRTS IPGPLQGDGQ DVATILHLVH
NLIHEEEEKE DKPSQQMQNV GEQAHMALLG HSLAAYISVL DRERLRKLTT RILSDTTLWL
CRLFRYENGS ACFHEDDRAG LVRVCRLVIN VRYEEFATEG YAVLSSKQPV IYQSSSCRPG
LGQHLCSQLG LPLSSLCTVP CNTIFGSQHQ MDVALLDKLI KEDIEAGKLP LLLIANAGTP
GAGHTDKLGR LKELCDQYNM WLHVEGVNLA TLALGQVTSA VMAATRSDSM TMTPGQWLGL
PAVTAVTLYR HEDPALSLAA GLTSSQPVEK LRALPLWLSL QHLGHNGIVQ KIKHATALSQ
QLLQKLKSMA SIKTSVEDEL NSPVVLFKFS QEMSAASSGG SVEGYCAGEK EVLDTFNRWL
GEQLAQLVPT SGVDVVELED EGTCVRFSPL LTAAVLGTQP EDVEELVERL SELVPVMSST
MCLRQDFREE SHRHSASLRY VDDISWPGLG VVRYEPQAEG MDESRRKQVL EKINNELLRK
LQDLDTDIIF STGPEFGAAK YTIFVGMVTE DVDVSELVDT IAALGRDIEE SGRLLENMTE
VVRKGILEAE LQLQKANEEK LIEEGMLRQI PLVGSVLNWF SPVESSIKGR TFNLAAGALN
STEMTYSTKA QAGRPSLQDT PTHSSKRLSG QRLFRRSGAN FDSFSETSSI GQADEMTREE
STTVSSSIQP PTSALAQEED LSSVSEIPPE KVQESSDQIH NTQVETEEAS EERQHEGREM
EQSGR
//
