ID A0KYP4_SHESA Unreviewed; 549 AA.
AC A0KYP4;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABK48913.1};
GN OrderedLocusNames=Shewana3_2686 {ECO:0000313|EMBL:ABK48913.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK48913.1, ECO:0000313|Proteomes:UP000002589};
RN [1] {ECO:0000313|Proteomes:UP000002589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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; CP000469; ABK48913.1; -; Genomic_DNA.
DR RefSeq; WP_011717571.1; NC_008577.1.
DR AlphaFoldDB; A0KYP4; -.
DR STRING; 94122.Shewana3_2686; -.
DR KEGG; shn:Shewana3_2686; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_6; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000002589; 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; 60829 MW; C0865B393CF637F6 CRC64;
MTQKLPRQAI ASEDSLMRIF TVPEDAESTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
TDFQAFEIPS QPRFVSDYTD EIMQNLVAHS VHTAAPSFIG HMTSALPYFV LPLSKMMVGL
NQNLVKIETS KAFTPLERQV LGMMHHLIYA QDDDFYRNWM HSANHSLGAF CSGGTVANIT
ALWIARNQLL KADGDFKGVT REGLIKALRH YGFDDLAILV SERGHYSLGK AVDLLGIGRD
NIISIPTDGN NKVDVAKMRE VAAELANKRI KVMAIVGVAG TTETGNIDPL RELAALASEL
NCHFHVDAAW GGASLLSNKY RHLLDGIELA DSVTIDAHKQ MYVPMGAGMV LFKNPEFAHA
IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFAE
QIDAHPDFEL VTAPELCLLT YRYVPAEVQA AMQVAIDQGD KVKLARFNEL LDGLTQFIQK
HQREQGKSFV SRTRIQPARY FRQPTVVFRV VLANPLTSHE ILNRVLIEQG EIAALDKEFL
PALLAMANE
//