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Database: UniProt/TrEMBL
Entry: Q0HTI2_SHESR
LinkDB: Q0HTI2_SHESR
Original site: Q0HTI2_SHESR 
ID   Q0HTI2_SHESR            Unreviewed;       549 AA.
AC   Q0HTI2;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   28-MAR-2018, entry version 72.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABI43573.1};
GN   OrderedLocusNames=Shewmr7_2588 {ECO:0000313|EMBL:ABI43573.1};
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI43573.1, ECO:0000313|Proteomes:UP000001960};
RN   [1] {ECO:0000313|Proteomes:UP000001960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7 {ECO:0000313|Proteomes:UP000001960};
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
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|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; CP000444; ABI43573.1; -; Genomic_DNA.
DR   RefSeq; WP_011626622.1; NC_008322.1.
DR   ProteinModelPortal; Q0HTI2; -.
DR   EnsemblBacteria; ABI43573; ABI43573; Shewmr7_2588.
DR   KEGG; shm:Shewmr7_2588; -.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   Proteomes; UP000001960; 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   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   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:UP000001960};
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;  60928 MW;  D424606D8E43EF47 CRC64;
     MTQKLPRQAI ASEDSLMRIF TVPEDAESTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
     TDFQAFEIPS QPRFVSDYTD EIMQNLVAHS VHTAAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHHLIYA QHDDFYRNWM HSANHSLGAF CSGGTVANIT
     ALWIARNQLL KADGDFKGVT REGLIKALRH YGFDDLAILV SERGHYSLGK AVDLLGIGRD
     NIISIPTDGN NKVDVAKMRE VAAELANKRI KIMAIVGVAG TTETGNIDPL RELAALASEL
     NCHFHVDAAW GGASLLSNKY RHLLDGIELA DSVTIDAHKQ MYVPMGAGMV LFKNPEFAHA
     IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFAE
     QIDAHPDFEL VTAPELCLLT YRYVPANVQA AMQLAIEQGY KTKLARFNEL LDGLTQFIQK
     HQREQGKSFV SRTRIQPARY FRQPTVVFRV VLANPLTSHE ILNQVLIEQG EIAALDKEFL
     PALLAMVNE
//
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