HIS6_SOLM1
ID HIS6_SOLM1 Reviewed; 259 AA.
AC C4XS73;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE Short=IGPS subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
GN Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013}; OrderedLocusNames=DMR_21040;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
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. {ECO:0000255|HAMAP-Rule:MF_01013}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01013};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000255|HAMAP-Rule:MF_01013}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC Rule:MF_01013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC Rule:MF_01013}.
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; AP010904; BAH75595.1; -; Genomic_DNA.
DR RefSeq; WP_015860781.1; NC_012796.1.
DR AlphaFoldDB; C4XS73; -.
DR SMR; C4XS73; -.
DR STRING; 573370.DMR_21040; -.
DR EnsemblBacteria; BAH75595; BAH75595; DMR_21040.
DR KEGG; dma:DMR_21040; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_7; -.
DR OMA; IFHYKET; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000009071; 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..259
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_1000213207"
FT ACT_SITE 11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
SQ SEQUENCE 259 AA; 27285 MW; 2784F9C377938EAE CRC64;
MLSKRVIPCL DVRDGKLTKG IKFQGNVDIG DPVETARLYY EAGADELVFY DITASSEGRG
IMLDVVDRVA REIFIPFSVG GGISTVEDMR AVLLAGAEKI SVNSAAVKNP DIISLGAAAF
GSQCVVVGMD VKHVGVSEQI PSGYEIVIHG GRKAMGLDAL EWARTVEALG AGEICCNSID
ADGAKTGYEL TLTRMIAEAV TIPVIASGGA GNPDHMADAV TTGKASAALI ASIVHYGEYS
IKDCKDHMAK RGVKVRNIW
