(data stored in SCRATCH zone)

SWISSPROT: Q13S99_PARXL

ID   Q13S99_PARXL            Unreviewed;       450 AA.
AC   Q13S99;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   SubName: Full=Putative pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABE33040.1};
GN   ORFNames=Bxe_B2955 {ECO:0000313|EMBL:ABE33040.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33040.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33040.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33040.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33040.1; -; Genomic_DNA.
DR   RefSeq; WP_011490429.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S99; -.
DR   STRING; 266265.Bxe_B2955; -.
DR   EnsemblBacteria; ABE33040; ABE33040; Bxe_B2955.
DR   GeneID; 4006797; -.
DR   KEGG; bxb:DR64_5286; -.
DR   KEGG; bxe:Bxe_B2955; -.
DR   PATRIC; fig|266265.5.peg.4732; -.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000121943; -.
DR   OMA; SAMWVKK; -.
DR   OrthoDB; POG091H05DC; -.
DR   Proteomes; UP000001817; Chromosome 2.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q13S99.
DR   SWISS-2DPAGE; Q13S99.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:UP000001817}.
FT   MOD_RES     285    285       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   450 AA;  48295 MW;  FB105C5CB2BF19F5 CRC64;
     MDELALAADA DRRAHAYLAG IGKRRVFPDA AALAQLAAFD EAFPQHGHAP ADVLRLLDES
     GTPATVASND PRYYGFVIGA VLPAAAAAER LMGAWDQCAS TFDNSPVAAT LEKIAARWVL
     DALDLPREAA IGFGTSATAC TLVCIAAARR ALLARKGWDF DNDGLDGAPP VRVVISEMAH
     ITVKKALRVL GFGMKRVVSA PVDEHGRIDP AQLPPLDDMT IFCVQAGEVN TGEFDPFAEL
     IPRAKAAGAW VHVDGAFGLW ARASSKRTLT EGIDGADSWT TDGHKWLNTP YDGAMAICRD
     ARALSAAMNS DAVYLSGAHD AQKNLNLEFS RRARGIPIWA ALRSLGRSGV QEMVDRHCAQ
     ASRIAEGLRA AGFEVVNRVV LNQVLVRANT DAQTVAIREA AQASGETWFG QTVWQGRPAF
     RISVSSWRTE DTHVDQLVAL LARLLAEQRA
//

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