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
//