ID HIS2_VIBPA Reviewed; 211 AA.
AC Q87QK5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=VP1144;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000031; BAC59407.1; -; Genomic_DNA.
DR RefSeq; NP_797523.1; NC_004603.1.
DR RefSeq; WP_005460001.1; NC_004603.1.
DR AlphaFoldDB; Q87QK5; -.
DR SMR; Q87QK5; -.
DR GeneID; 1188649; -.
DR KEGG; vpa:VP1144; -.
DR PATRIC; fig|223926.6.peg.1086; -.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_6; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000002493; Chromosome 1.
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; 1.10.287.1080; MazG-like; 1.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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 NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 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_0000136446"
FT REGION 1..122
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 123..211
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ SEQUENCE 211 AA; 23254 MW; BF76B59DF60FD27E CRC64;
MSFKAAEVSS LSERINWEKV DGLVPAIVQD FQSSQVLMMG YMNQDALAKT GETGQVTFFS
RTKERLWTKG ETSGNVLQLV NISLDCDNDT LLVRVNPIGP TCHTGTTTCW DGDAQEESQM
VWLHQLEQLL AARKSADPDS SYTASLYARG TKRISQKVGE EGVEVALAAT SGDKAELVCE
SADLIYHLLV LLQDQGLSMN DVVNKLKERH K
//
