HIS2_GLOVI
ID HIS2_GLOVI Reviewed; 218 AA.
AC Q7NLB5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=glr1211;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC89152.1; -; Genomic_DNA.
DR RefSeq; NP_924157.1; NC_005125.1.
DR RefSeq; WP_011141211.1; NC_005125.1.
DR AlphaFoldDB; Q7NLB5; -.
DR SMR; Q7NLB5; -.
DR STRING; 251221.35211775; -.
DR EnsemblBacteria; BAC89152; BAC89152; BAC89152.
DR KEGG; gvi:glr1211; -.
DR PATRIC; fig|251221.4.peg.1235; -.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_3; -.
DR InParanoid; Q7NLB5; -.
DR OMA; ERSCFHQ; -.
DR OrthoDB; 1842189at2; -.
DR PhylomeDB; Q7NLB5; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000000557; 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_01021; HisI; 1.
DR HAMAP; MF_01019; HisIE; 1.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR026660; PRA-CH.
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..218
FT /note="Histidine biosynthesis bifunctional protein HisIE"
FT /id="PRO_0000136414"
FT REGION 1..131
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 132..218
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ SEQUENCE 218 AA; 24795 MW; C481BA9FC121EC17 CRC64;
MAPHQFKSKG APTLVHVREA ARFDRDGLIP AVVQDVLDGT VLMVAWMNRE ALERTLETGE
SWFWSRSRQE LWHKGATSGH RQKIKALRYD CDSDVLLLTV EQQGDIACHL GERSCFHRDE
AGDYDLPPAD TLSQVFRVVE ERKAHPHPDS YTSRLLEAGS NKILKKIGEE ATEVVMAAKD
GERVAEEVAD LWYHTLVLLA HADVDILDVY RALQQRRR
