ID A0A3Q3B3U4_KRYMA Unreviewed; 552 AA.
AC A0A3Q3B3U4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acidic amino acid decarboxylase GADL1-like {ECO:0000313|Ensembl:ENSKMAP00000023710.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000023710.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000023710.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR AlphaFoldDB; A0A3Q3B3U4; -.
DR STRING; 37003.ENSKMAP00000023710; -.
DR Ensembl; ENSKMAT00000024012.1; ENSKMAP00000023710.1; ENSKMAG00000017536.1.
DR GeneTree; ENSGT00940000158391; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 1.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF1; ACIDIC AMINO ACID DECARBOXYLASE GADL1; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 552 AA; 62932 MW; D2C37AC24DC80E3B CRC64;
MRSRCGGRGR RDRKTTEVNS DKTGRTQKLK RQPNQDQQET PDKEQNPNNT NIHDTVCNLY
DVPLNGPALS VLSVDSFIHQ SMGIILEDAV KKATDVREKV CEWRSPEELK ELLDLELRDQ
GESESKILKR CRDAIRYSVK TTHPRFFNQL FAGMEPYSLV ASFITETLKT SLYTYEMAPV
FTLIEDAVLR KMMEMIGWEE GGDGIFNAGG SMSNMYAMNL ARYRYYPDIK ELGLSAAPQL
AVFTSQESHY SISKAAALMG IGTKNVHMVP TDKRGKMIPS ALEEQIESAK RKVRTVPFLV
NATAGTTVFG AFDPIDKIGE ICEKHNLWLH VDACWGGGAL MSKKHKYLLK GIEKANSVAW
NPHKMLMTCL QCSAFLIRDK THLLQHCHSA RASYLFQQDK FYDVSYDIGD KSIQCSRKPD
AFKFWLTWKA LGTKELGQRV DRAFEMSRYL AEEIKKREGF RLLMEPEYAN VCFWYIPPSL
RNLPDGPEFC QKLHNVAPVI KERMMKMGSM MVGYQPHGGN ANFFRMVVIS PQVSRQDLDF
VLDEIHNLGK DL
//
