ID   HIS2_SHEON              Reviewed;         211 AA.
AC   Q8EFB6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Histidine biosynthesis bifunctional protein hisIE;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE              Short=PRA-CH;
DE              EC=3.5.4.19;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE              Short=PRA-PH;
DE              EC=3.6.1.31;
GN   Name=hisI; Synonyms=hisIE; OrderedLocusNames=SO_2067;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5-
CC       phosphoribosyl)-AMP + diphosphate.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-
CC       phosphoribosyl)-5-((5-
CC       phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH
CC       family.
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DR   EMBL; AE014299; AAN55114.1; -; Genomic_DNA.
DR   RefSeq; NP_717670.1; -.
DR   GeneID; 1169812; -.
DR   GenomeReviews; AE014299_GR; SO_2067.
DR   KEGG; son:SO_2067; -.
DR   NMPDR; fig|211586.1.peg.1879; -.
DR   TIGR; SO_2067; -.
DR   HOGENOM; Q8EFB6; -.
DR   OMA; Q8EFB6; VHYWSRS.
DR   BioCyc; SONE211586:SO_2067-MON; -.
DR   BRENDA; 3.5.4.19; 257422.
DR   BRENDA; 3.6.1.31; 257422.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:HAMAP.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01019; -; 1.
DR   InterPro; IPR002496; PRA_CycHdrlase.
DR   InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   ProDom; PD002610; PRA_cyclohydro; 1.
DR   ProDom; PD002611; Pra_PH/CH; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding.
FT   CHAIN         1    211       Histidine biosynthesis bifunctional
FT                                protein hisIE.
FT                                /FTId=PRO_0000136428.
FT   REGION        1    117       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      118    211       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   211 AA;  23166 MW;  6019DF853BDAC26E CRC64;
     MSTQTNTKSD FSELDWDKQD GLIPAVIQNH LSGKVLMLGY MDKAALEQTL ATGDVTFFSR
     SKQRLWTKGE TSGHTLKLVA IDKDCDNDSL LVQVLPNGPT CHKGTESCWL DGNAHPFLNN
     LAELIASRKG QSPESSYTAS LFARGTKRIA QKVGEEGLET ALAAATHDKE ELVNEASDLM
     YHLLVLLEDQ ALSLSDITAN LLARHQKAQR K
//