ID   HIS2_VIBVY              Reviewed;         211 AA.
AC   Q7MLS0;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
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}; OrderedLocusNames=VV1357;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94121.1; -; Genomic_DNA.
DR   RefSeq; WP_011150024.1; NC_005139.1.
DR   AlphaFoldDB; Q7MLS0; -.
DR   SMR; Q7MLS0; -.
DR   STRING; 672.VV93_v1c12700; -.
DR   EnsemblBacteria; BAC94121; BAC94121; BAC94121.
DR   KEGG; vvy:VV1357; -.
DR   PATRIC; fig|196600.6.peg.1346; -.
DR   eggNOG; COG0139; Bacteria.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_048577_3_1_6; -.
DR   OMA; ERSCFHQ; -.
DR   OrthoDB; 1842189at2; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT   CHAIN           1..211
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136448"
FT   REGION          1..122
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          123..211
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ   SEQUENCE   211 AA;  23220 MW;  A6440E671C35469B CRC64;
     MSVKAAEVSS LAERINWEKV DGLVPAIVQD FQSSQVLMMG YMNQDALAKT GETGQVTFFS
     RTKERLWTKG ETSGNVLQLV NMSLDCDNDT LLVKVNPIGP TCHTGTTTCW DGDPQEESQM
     VWLHQLEQLL AARKSADPDS SYTASLYARG TKRISQKVGE EGVEVALAAT SGDKAELVCE
     SADLIYHLLV LLQDQGLSMN DVINKLKERH K