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HIS6_RHIME
ID   HIS6_RHIME              Reviewed;         258 AA.
AC   Q92TB3;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=R00051; ORFNames=SMc02569;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(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 (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}.
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DR   EMBL; AL591688; CAC41438.1; -; Genomic_DNA.
DR   RefSeq; NP_384157.1; NC_003047.1.
DR   RefSeq; WP_010968318.1; NC_003047.1.
DR   AlphaFoldDB; Q92TB3; -.
DR   SMR; Q92TB3; -.
DR   STRING; 266834.SMc02569; -.
DR   EnsemblBacteria; CAC41438; CAC41438; SMc02569.
DR   GeneID; 61601526; -.
DR   KEGG; sme:SMc02569; -.
DR   PATRIC; fig|266834.11.peg.1405; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_5; -.
DR   OMA; IFHYKET; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001976; 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;
KW   Reference proteome.
FT   CHAIN           1..258
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_0000142217"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  27312 MW;  56125BFBF22F39D3 CRC64;
     MTLKARVIPC LDVKDGRVVK GVNFVDLIDA GDPVEAARAY DAAGADELCF LDITASSDNR
     ETIFDVVART AEQCFMPLTV GGGVRQVADI RKLLLAGADK VSINTAAVKN PEFVAEAADK
     FGDQCIVVAI DAKKVSAQGE ADRWEIFTHG GRQPTGIDAI EFARKVVDLG AGEILLTSMD
     RDGTKSGYDI SLTRAIADAV RAPVIASGGV GTLDHMVEGI RDGHATAVLA ASIFHFGTYS
     IGEAKRHMAK HGIAMRLD
 
 
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