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HIS2_XANAC
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   25-MAY-2022, entry version 108.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisIE {ECO:0000255|HAMAP-Rule:MF_01019};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01019};
DE              Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01019};
DE              EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01019};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01019};
DE              Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01019};
DE              EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01019};
GN   Name=hisI {ECO:0000255|HAMAP-Rule:MF_01019};
GN   Synonyms=hisIE {ECO:0000255|HAMAP-Rule:MF_01019};
GN   OrderedLocusNames=XAC1835;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   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., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC         ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC         D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC         ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01019};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01019}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01019}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01019}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01019}.
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DR   EMBL; AE008923; AAM36697.1; -; Genomic_DNA.
DR   RefSeq; WP_003486226.1; NC_003919.1.
DR   AlphaFoldDB; Q8PLG5; -.
DR   SMR; Q8PLG5; -.
DR   STRING; 190486.XAC1835; -.
DR   PRIDE; Q8PLG5; -.
DR   EnsemblBacteria; AAM36697; AAM36697; XAC1835.
DR   GeneID; 66910981; -.
DR   KEGG; xac:XAC1835; -.
DR   eggNOG; COG0139; Bacteria.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_048577_3_1_6; -.
DR   OMA; ERSCFHQ; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000000576; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR   Gene3D; 3.10.20.810; -; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   HAMAP; MF_01019; HisIE; 1.
DR   InterPro; IPR023019; His_synth_HisIE.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW   Hydrolase; Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN           1..206
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136450"
FT   REGION          1..117
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          118..206
FT                   /note="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
 
 
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