HIS6_BUCAP
ID HIS6_BUCAP Reviewed; 258 AA.
AC Q9ZHE1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=BUsg_098;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9767718; DOI=10.1007/s002849900392;
RA Clark M.A., Baumann L., Baumann P.;
RT "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes
RT of histidine biosynthesis.";
RL Curr. Microbiol. 37:356-358(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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 (By similarity). {ECO:0000250}.
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 -!- 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF067228; AAC97360.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67668.1; -; Genomic_DNA.
DR RefSeq; WP_011053634.1; NC_004061.1.
DR AlphaFoldDB; Q9ZHE1; -.
DR SMR; Q9ZHE1; -.
DR STRING; 198804.BUsg_098; -.
DR EnsemblBacteria; AAM67668; AAM67668; BUsg_098.
DR KEGG; bas:BUsg_098; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_6; -.
DR OMA; IFHYKET; -.
DR OrthoDB; 1522718at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase.
FT CHAIN 1..258
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142134"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT CONFLICT 55
FT /note="S -> C (in Ref. 1; AAC97360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28771 MW; BC7EB15E3A7F90F4 CRC64;
MLAKRIIACL DVNNGVVVKG IQFKNHEIVG DIISLSKRYT KEGIDELVFY DITASTNNKL
VDRSWIKKVA EIINIPFCVA GGIKSVEDAQ NILSFGADKI SINSSALIDP DLITKIANRF
GVQCTVVGID SWFDSDKKKY MVQQYTGDAN RTYQTDWETI DWVEKVQKKG AGEIVLNMMN
QDGLQNGYDL SQLNEIRKKC KVPLIASGGA GCADHFYQAF DHANVDGVLA ASVFHKKIVN
IKDLKYFLIQ KGLEIRIC
