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Database: UniProt/TrEMBL
Entry: A0KYP4_SHESA
LinkDB: A0KYP4_SHESA
Original site: A0KYP4_SHESA 
ID   A0KYP4_SHESA            Unreviewed;       549 AA.
AC   A0KYP4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   07-JUN-2017, entry version 59.
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; Proteobacteria; 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.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   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|PIRSR:PIRSR602129-50,
CC         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   ProteinModelPortal; A0KYP4; -.
DR   STRING; 94122.Shewana3_2686; -.
DR   EnsemblBacteria; ABK48913; ABK48913; Shewana3_2686.
DR   KEGG; shn:Shewana3_2686; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; SSP94122:GJ9K-2778-MONOMER; -.
DR   Proteomes; UP000002589; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002589};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     339    339       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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