HIS6_ECOLI
ID HIS6_ECOLI Reviewed; 258 AA.
AC P60664; P10373;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF;
DE EC=4.3.2.10;
DE AltName: Full=IGP synthase cyclase subunit;
DE AltName: Full=IGP synthase subunit HisF;
DE AltName: Full=ImGP synthase subunit HisF;
DE Short=IGPS subunit HisF;
GN Name=hisF; OrderedLocusNames=b2025, JW2007;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-258.
RC STRAIN=O9:K31-:H- / F719;
RX PubMed=7536735; DOI=10.1128/jb.177.8.2178-2187.1995;
RA Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T.,
RA Kato N., Jann K.;
RT "Expression of the O9 polysaccharide of Escherichia coli: sequencing of the
RT E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and
RT evidence for an ATP-binding cassette transport system.";
RL J. Bacteriol. 177:2178-2187(1995).
RN [6]
RP PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=8494895; DOI=10.1021/bi00070a029;
RA Klem T.J., Davisson V.J.;
RT "Imidazole glycerol phosphate synthase: the glutamine amidotransferase in
RT histidine biosynthesis.";
RL Biochemistry 32:5177-5186(1993).
RN [7]
RP MUTAGENESIS OF ARG-5; GLU-46; GLN-123 AND CYS-124.
RX PubMed=11208798; DOI=10.1128/jb.182.3.989-996.2001;
RA Klem T.J., Chen Y., Davisson V.J.;
RT "Subunit interactions and glutamine utilization by Escherichia coli
RT imidazole glycerol phosphate synthase.";
RL J. Bacteriol. 183:989-996(2001).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The HisF subunit catalyzes the cyclization
CC activity that produces IGP and AICAR from PRFAR using the ammonia
CC provided by the HisH subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC ChEBI:CHEBI:58525; EC=4.3.2.10;
CC Evidence={ECO:0000269|PubMed:8494895};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=240 uM for PRFAR {ECO:0000269|PubMed:8494895};
CC KM=23 uM for NH(4)Cl {ECO:0000269|PubMed:8494895};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:8494895};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000269|PubMed:8494895}.
CC -!- INTERACTION:
CC P60664; P60595: hisH; NbExp=2; IntAct=EBI-9151168, EBI-1126953;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; X13462; CAA31817.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75086.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15857.1; -; Genomic_DNA.
DR EMBL; D43637; BAA07754.1; -; Genomic_DNA.
DR PIR; JS0134; OYECHF.
DR RefSeq; NP_416529.1; NC_000913.3.
DR RefSeq; WP_000880182.1; NZ_SSUR01000003.1.
DR AlphaFoldDB; P60664; -.
DR SMR; P60664; -.
DR BioGRID; 4259164; 22.
DR BioGRID; 850865; 4.
DR ComplexPortal; CPX-5158; Imidazole glycerol phosphate synthase complex.
DR IntAct; P60664; 5.
DR STRING; 511145.b2025; -.
DR jPOST; P60664; -.
DR PaxDb; P60664; -.
DR PRIDE; P60664; -.
DR EnsemblBacteria; AAC75086; AAC75086; b2025.
DR EnsemblBacteria; BAA15857; BAA15857; BAA15857.
DR GeneID; 946516; -.
DR KEGG; ecj:JW2007; -.
DR KEGG; eco:b2025; -.
DR PATRIC; fig|1411691.4.peg.227; -.
DR EchoBASE; EB0443; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_6; -.
DR InParanoid; P60664; -.
DR OMA; IFHYKET; -.
DR PhylomeDB; P60664; -.
DR BioCyc; EcoCyc:CYCLASE-MON; -.
DR BioCyc; MetaCyc:CYCLASE-MON; -.
DR BRENDA; 4.3.1.B2; 2026.
DR UniPathway; UPA00031; UER00010.
DR PRO; PR:P60664; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009382; C:imidazoleglycerol-phosphate synthase complex; IDA:EcoCyc.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IDA:EcoCyc.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:ComplexPortal.
DR CDD; cd04731; HisF; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01013; HisF; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00735; hisF; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing;
KW Histidine biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..258
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142156"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT MUTAGEN 5
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 5
FT /note="R->H: Loss of IGP synthase activity. Weak IGP
FT synthase activity and reduced HisH activity in vitro."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 46
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 46
FT /note="E->G: Loss of IGP synthase activity. Weak IGP
FT synthase and HisH activities in vitro."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 123
FT /note="Q->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 123
FT /note="Q->R: Loss of IGP synthase activity. Weak HisH
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 124
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:11208798"
FT MUTAGEN 124
FT /note="C->R: Loss of IGP synthase activity. Weak HisH
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:11208798"
SQ SEQUENCE 258 AA; 28454 MW; FCE14A345521BEA1 CRC64;
MLAKRIIPCL DVRDGQVVKG VQFRNHEIIG DIVPLAKRYA EEGADELVFY DITASSDGRV
VDKSWVSRVA EVIDIPFCVA GGIKSLEDAA KILSFGADKI SINSPALADP TLITRLADRF
GVQCIVVGID TWYDAETGKY HVNQYTGDES RTRVTQWETL DWVQEVQKRG AGEIVLNMMN
QDGVRNGYDL EQLKKVREVC HVPLIASGGA GTMEHFLEAF RDADVDGALA ASVFHKQIIN
IGELKAYLAT QGVEIRIC
