ID   HIS4_BURTA              Reviewed;         251 AA.
AC   Q2SUA7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE            EC=5.3.1.16;
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN   Name=hisA; OrderedLocusNames=BTH_I2988;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-5-((5-
CC       phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-
CC       ((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-
CC       phosphoribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the hisA/hisF family.
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DR   EMBL; CP000086; ABC37752.1; -; Genomic_DNA.
DR   RefSeq; YP_443492.1; -.
DR   GeneID; 3847621; -.
DR   GenomeReviews; CP000086_GR; BTH_I2988.
DR   KEGG; bte:BTH_I2988; -.
DR   TIGR; BTH_I2988; -.
DR   HOGENOM; Q2SUA7; -.
DR   OMA; Q2SUA7; VATRGWL.
DR   BioCyc; BTHA271848:BTH_I2988-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylam...; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01014; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006063; His4.
DR   InterPro; IPR006062; His_biosynth.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   TIGRFAMs; TIGR00007; His4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Isomerase.
FT   CHAIN         1    251       1-(5-phosphoribosyl)-5-[(5-
FT                                phosphoribosylamino)methylideneamino]
FT                                imidazole-4-carboxamide isomerase.
FT                                /FTId=PRO_0000290458.
FT   ACT_SITE      8      8       Proton acceptor (By similarity).
FT   ACT_SITE    131    131       Proton donor (By similarity).
SQ   SEQUENCE   251 AA;  26588 MW;  C40580F9C7E013FE CRC64;
     MLLIPAIDLK DGQCVRLKQG DMDQATIFSE DPAAMARKWV DLGARRLHLV DLNGAFAGKP
     KNLEAIEAIL GEVGDEIPVQ LGGGIRSLET IEKYLDAGLS YVIIGTAAVK DPGFLRDACS
     AFAGNIIVGL DAKDGKVATD GWSKLTGHEV IDLAQKFEDY GVESIVYTDI GRDGMLQGIN
     IEATVKLAQA VGIPVIASGG LSNIVDIEKL CEVEDEGIEG VICGRAIYSG DLDFAAAQKR
     ADELNGELDD A
//