ID   ULAD_SHIF8              Reviewed;         216 AA.
AC   Q0SX89;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase ulaD;
DE            EC=4.1.1.85;
DE   AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase;
DE   AltName: Full=KGPDC;
DE   AltName: Full=L-ascorbate utilization protein D;
GN   Name=ulaD; OrderedLocusNames=SFV_4352;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P
CC       into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate
CC       utilization (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3-dehydro-L-gulonate 6-phosphate = L-xylulose
CC       5-phosphate + CO(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Cofactor degradation; L-ascorbic acid degradation; D-
CC       xylulose 5-phosphate from L-ascorbic acid: step 2/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by ulaR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
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DR   EMBL; CP000266; ABF06326.1; -; Genomic_DNA.
DR   RefSeq; YP_691631.1; -.
DR   SMR; Q0SX89; 2-216.
DR   GeneID; 4208607; -.
DR   GenomeReviews; CP000266_GR; SFV_4352.
DR   KEGG; sfv:SFV_4352; -.
DR   HOGENOM; Q0SX89; -.
DR   OMA; Q0SX89; PIYIFIA.
DR   BioCyc; SFLE373384:SFV_4352-MON; -.
DR   GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxyl...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:HAMAP.
DR   HAMAP; MF_01267; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001754; OMPdecase_core.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00215; OMPdecase; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Complete proteome; Decarboxylase; Lyase;
KW   Magnesium; Metal-binding.
FT   CHAIN         1    216       3-keto-L-gulonate-6-phosphate
FT                                decarboxylase ulaD.
FT                                /FTId=PRO_1000067321.
FT   METAL        33     33       Magnesium (By similarity).
FT   METAL        62     62       Magnesium (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
FT   BINDING     192    192       Substrate (By similarity).
FT   SITE         64     64       Transition state stabilizer (By
FT                                similarity).
FT   SITE         67     67       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   216 AA;  23649 MW;  CDF287AC1D1BAD68 CRC64;
     MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL
     ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE
     QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF
     KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG
//