ID R8AUM7_PLESH Unreviewed; 568 AA.
AC R8AUM7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Decarboxylase, group II {ECO:0000313|EMBL:EON90037.1};
GN ORFNames=PLESHI_00872 {ECO:0000313|EMBL:EON90037.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON90037.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON90037.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON90037.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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}.
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:EON90037.1}.
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DR EMBL; AQQO01000021; EON90037.1; -; Genomic_DNA.
DR RefSeq; WP_010861814.1; NZ_KB944507.1.
DR AlphaFoldDB; R8AUM7; -.
DR STRING; 703.SAMEA2665130_01254; -.
DR PATRIC; fig|1315976.3.peg.149; -.
DR HOGENOM; CLU_034727_0_0_6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000014012; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT MOD_RES 360
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 568 AA; 64859 MW; BB3F7D90F81BA3E4 CRC64;
MNQHDMWLNS AEANDVSSYF SGRYRQVMDW FFSRDPKHWP VYQDPGFQQI NAFRQKHLAP
AERLAAYPQG ERFFAEIESL SAVKPRMHQP GSGPDPLLTF AAAMSKDWEN PSSVENVITM
PCDPAVYGAM MCSLANPNLA YCEYAGMADH LEKTVIRQVA TLAGYDPAQA TGVFTQGGTF
CNLYGYLLGI RKSLPEARTL GMGVDQDYRI INSQGGHYSN MTNLSLLGVD IRHKTIRIKV
TESNDIDLVD LERQMRACFD VHCKIPAIML TLGTTDTFGV DRIKPVYDLR NRLCDEYDIA
VKPHIHADAA VGWSMLFFLD YEFDRNPLEI NESTLAGIRH NVERFREVKY ADSFTVDFQK
WGYVPYTSSL VMIKNRDDMH ALENDPENFS YFEHDLQGQT HLQSTIECSR GAAGMFGAFS
ALQHMGIEGY QIILAHCLQN ANYFRHQLQQ LGNVKLMVPE NQGPSVGFKV YDPNCVQDPE
AEFLLEQSCM SDPQAMERMK RNSHYHREQF MQRGKFGLYT NWVEFIARSS YNAKGAYAYI
PGEKAVFMNP ATGREQIDQF IQRMKQFR
//
