ID A0A1X7KMD8_9BACT Unreviewed; 307 AA.
AC A0A1X7KMD8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyridoxal-dependent decarboxylase conserved domain-containing protein {ECO:0000313|EMBL:SMG42337.1};
GN ORFNames=SAMN05661096_02887 {ECO:0000313|EMBL:SMG42337.1};
OS Marivirga sericea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=1028 {ECO:0000313|EMBL:SMG42337.1, ECO:0000313|Proteomes:UP000193804};
RN [1] {ECO:0000313|EMBL:SMG42337.1, ECO:0000313|Proteomes:UP000193804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4125 {ECO:0000313|EMBL:SMG42337.1,
RC ECO:0000313|Proteomes:UP000193804};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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 ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR EMBL; FXAW01000006; SMG42337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7KMD8; -.
DR STRING; 1028.SAMN05661096_02887; -.
DR Proteomes; UP000193804; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 165
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 307 AA; 35010 MW; DB6D3AA62463B07F CRC64;
MYCDTDYDGY VASGGTEANM QAVWIYRNYY KQEHQAKLDE IALISSADAH YSSAKASNVL
QIDFYKVAVD ENDRSISKQA LENTLAQAQQ DGKKYFIIMA NMMTTMFGSV DDVNIYTDVL
TDKGLDFKLH VDGAYGGFFY PFAKPKNALN FSNSHVNSVT LDAHKMLQAP YGTGIFLIRK
NWMHYANTQE ASYVEGQDFT LIGSRSGANA IAIWMILMTY GPNGWFEKTL VLNHRTEWLC
KALKAKSIAY YRYPEANIVT IKAEFLNKEV CKKYGLIPDS HQNPMWYKIV VMDHVTIEKL
EQFLEEV
//
