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Database: UniProt
Entry: A0A432W486_9GAMM
LinkDB: A0A432W486_9GAMM
Original site: A0A432W486_9GAMM 
ID   A0A432W486_9GAMM        Unreviewed;       589 AA.
AC   A0A432W486;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Putative pyridoxal-dependent aspartate 1-decarboxylase {ECO:0000313|EMBL:RUO24279.1};
GN   Name=panP {ECO:0000313|EMBL:RUO24279.1};
GN   ORFNames=CWE09_10390 {ECO:0000313|EMBL:RUO24279.1};
OS   Aliidiomarina minuta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=880057 {ECO:0000313|EMBL:RUO24279.1, ECO:0000313|Proteomes:UP000288293};
RN   [1] {ECO:0000313|EMBL:RUO24279.1, ECO:0000313|Proteomes:UP000288293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLST1 {ECO:0000313|EMBL:RUO24279.1,
RC   ECO:0000313|Proteomes:UP000288293};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUO24279.1}.
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DR   EMBL; PIPL01000002; RUO24279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432W486; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000288293; 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; IPR022517; Asp_decarboxylase_pyridox.
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   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288293}.
FT   MOD_RES         377
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   589 AA;  64826 MW;  8067A4E36ECC6F6C CRC64;
     MSIPLLRLLN ANIRQQTSRC GSYKVTCAKV CAHANSRRCL LSNSSAADVS LDALYRIFTI
     PEAPDSTLGR IERHLSENLA GFLSDHIVAK EKPLHEIEED FADSEIPEQP TFVSEHTDEL
     LNKLVAHSVH TASPRFIGHM TSALPYFLLP LAKLMVGLNQ NLVKIETSKA FTPLERQVLG
     MMHHLVYGEQ EKFYQHWMHS AEHSLGAFCS GGTVANITAL WVARNKLFAA QPGFAGVATE
     GLAAGLQHYG YKKACVMVSE RGHYSLSKAA DVLGIGRANL VAIATDKNNR MDIEALRKGC
     QQIADEGGRV MALVGIAGTT ETGHIDPLEK MADVAAEIGA HFHVDAAWGG ATLLSSTHRG
     LLQGIERADS VTIDAHKQMY VPMGAGMVLF RDPALVHAIE HHAEYVIRRG SKDLGSHTME
     GSRPGMAMLV YSALHVMGRR GYQLLIDQSI DKAQAFSALI HQQPDFEVVT EPELCLLTYR
     YVPADIKEVL ANANEEQMNR ITPILNQLTK HVQKSQRESG NAFVSRTKLT PHQYFHQPST
     VFRTVLANPL TTMQMLSEIL EEQREIGENA PHTLHALYAE ARDCGLLSG
//
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