ID   HIS2_XANAC              Reviewed;         206 AA.
AC   Q8PLG5;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 52.
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=XAC1835;
OS   Xanthomonas axonopodis pv. citri (Citrus canker).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=92829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(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; AE008923; AAM36697.1; -; Genomic_DNA.
DR   RefSeq; NP_642161.1; NC_003919.1.
DR   ProteinModelPortal; Q8PLG5; -.
DR   SMR; Q8PLG5; 16-112, 117-205.
DR   GeneID; 1155906; -.
DR   GenomeReviews; AE008923_GR; XAC1835.
DR   KEGG; xac:XAC1835; -.
DR   NMPDR; fig|190486.1.peg.1805; -.
DR   HOGENOM; HBG294308; -.
DR   OMA; VMACKDD; -.
DR   ProtClustDB; PRK02759; -.
DR   BioCyc; XAXO190486:XAC1835-MONOMER; -.
DR   BRENDA; 3.5.4.19; 289771.
DR   BRENDA; 3.6.1.31; 289771.
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:EC.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01019; HisIE; 1; -.
DR   InterPro; IPR023019; His_synth_HisIE.
DR   InterPro; IPR008179; PRib-ATP_PPHydrolase.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 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    206       Histidine biosynthesis bifunctional
FT                                protein HisIE.
FT                                /FTId=PRO_0000136450.
FT   REGION        1    117       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      118    206       Phosphoribosyl-ATP pyrophosphohydrolase.
SQ   SEQUENCE   206 AA;  22262 MW;  1B04984CEEFBD377 CRC64;
     MGSNEVATGD PLATLDWNKG EGLLPVIVQD ADNLRVLMLG YMNAQALAVT QQRGEVTFFS
     RSKQRLWTKG ESSGNVLRVV SIQTDCDADT LLVQARPHGP TCHLGRTSCF PSAPGQFLGS
     LDALVAERER ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQDDD ALLGESADLL
     YHLIVLLRAR GLGLGDAAAL LESRHQ
//