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Database: UniProt/TrEMBL
Entry: A3QG03_SHELP
LinkDB: A3QG03_SHELP
Original site: A3QG03_SHELP 
ID   A3QG03_SHELP            Unreviewed;       546 AA.
AC   A3QG03;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABO24401.1};
GN   OrderedLocusNames=Shew_2535 {ECO:0000313|EMBL:ABO24401.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO24401.1, ECO:0000313|Proteomes:UP000001558};
RN   [1] {ECO:0000313|EMBL:ABO24401.1, ECO:0000313|Proteomes:UP000001558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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; CP000606; ABO24401.1; -; Genomic_DNA.
DR   RefSeq; WP_011866332.1; NC_009092.1.
DR   ProteinModelPortal; A3QG03; -.
DR   STRING; 323850.Shew_2535; -.
DR   EnsemblBacteria; ABO24401; ABO24401; Shew_2535.
DR   KEGG; slo:Shew_2535; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; SLOI323850:GHQJ-2616-MONOMER; -.
DR   Proteomes; UP000001558; 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:UP000001558};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001558}.
FT   MOD_RES     339    339       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   546 AA;  60147 MW;  26DCF164EB700BCE CRC64;
     MTSKQTRQAT ASEEALMRIF TLPEAPNSTL GKIEKNLSEN LMGFLKESIV AVEKPLTEIE
     KDFQAYQIPT APSFVSDYAE QMMQTLIAHS VHTSAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHHMVYG QTEEFYQSWM HSASHSLGAF CSGGTVANIT
     ALWIARNRLL KPDGDFKGVA QSGLMRALRH YGYDDLAILV STRGHYSLGK AADLLGIGRD
     NIISVPCASD NKVDVAKMRE AAEQLAEQNI KVMAIVGVAG TTETGNIDPL DELANLAEQL
     GCHFHVDAAW GGASLLSSKY RHLLAGIERA DSVTIDAHKQ MYVPMGAGMV LFKDPEFANA
     IKHHAEYILR KGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFGE
     LIAAQDDFQL VSRPELCLLT YRYVPAKVQA QLNEAVAAGD AARVSEINAL LDGLTKFIQK
     RQREQGKSFV SRTRIIPANN LEQTSVVFRV VLANPLTSNE ILQQVLDEQR DIAKLDDRFL
     PKLLAL
//
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