ID   E6XFR1_SHEP2            Unreviewed;       549 AA.
AC   E6XFR1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADV53943.1};
GN   OrderedLocusNames=Sput200_1479 {ECO:0000313|EMBL:ADV53943.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV53943.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV53943.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV53943.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA   Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-2011) 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.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP002457; ADV53943.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6XFR1; -.
DR   KEGG; shp:Sput200_1479; -.
DR   PATRIC; fig|399804.5.peg.1518; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000008209; Chromosome.
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}.
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  60764 MW;  8DC902710802647A CRC64;
     MTQKLPRQAT ASEESLMRIF TVPEDAESTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
     TDFQAFKIPT QPRFVSDYTD EIMQNLVAHS VHTSAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHQLIYA QDTDFYQSWM HSANHSLGAF CSGGTVANIT
     ALWIARNQLL KADGEFKGVT REGLLKALRY YGYDDLAILV SERGHYSLGK AVDLLGIGRD
     NIISIPTDSH NKVDIAKMRE AALELARKNI KVLAIVGVAG TTETGNVDPL IELAALAKEL
     NCHFHVDAAW GGASLLSNKY RHLLAGIELA DSVTIDAHKQ MYVPMGAGMV LFKNPEFAHA
     IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG LDGYEILINN SIEKARYFAE
     QIKAHKDFEL VTEPELCLLT YRYVPAKVQA AMQVAIEQGD TAKLARFNEL LDGLTQFIQK
     HQREQGKSFV SRTRISPARY FRQATVVFRV VLANPLTSHE ILNQVLVEQS EIAALDKEFL
     PALLAMVAE
//