ID   Q07ZT1_SHEFN            Unreviewed;       546 AA.
AC   Q07ZT1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABI72484.1};
GN   OrderedLocusNames=Sfri_2643 {ECO:0000313|EMBL:ABI72484.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72484.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI72484.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72484.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI72484.1; -; Genomic_DNA.
DR   RefSeq; WP_011638093.1; NC_008345.1.
DR   AlphaFoldDB; Q07ZT1; -.
DR   STRING; 318167.Sfri_2643; -.
DR   DNASU; 4279550; -.
DR   KEGG; sfr:Sfri_2643; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000000684; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684}.
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   546 AA;  60098 MW;  0C13A2BE828051C1 CRC64;
     MTSKITRQAN ASEDSLLRIF TAPEDSTSTL SIIEQKLSQD LAGFLGNSIA ALEKPLSEIE
     TDFSAYQIPT EPKFVSDYAD EIMQNLVAHS VHTSAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHNLVYQ QSDDFYHQWM HSANHSLGAF CSGGTVANIT
     ALWIARNRLL QPRGDFKGVT REGMTKALRF YGYDDLAILV SDRGHYSLGK TADLLGIGRD
     NIISIPTDEH HKVDVAAMRD AAEKLAQQNI KVMAIVGIAG TTETGNVDPL TELAALASEL
     NCHFHVDAAW GGASLLSKKY SHLLKGIELA DSVTIDAHKQ MYVPMGAGMV LFKDPELAKA
     IVHHAEYILR VGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFGS
     IIDQHADFEL VTAPELCLLT YRYVPKSVQA ILTTALANQD SALVASINEL LDGLTQFIQK
     HQREQGKSFV SRTRIKPAKY LRQPTTVFRV VLANPLTSHQ ILHDVLTEQV EIAALDSEYL
     PQLLAL
//