ID F6DPJ2_DESRL Unreviewed; 252 AA.
AC F6DPJ2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE EC=4.3.2.10 {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
DE Short=IGPS subunit HisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN Name=hisF {ECO:0000256|HAMAP-Rule:MF_01013};
GN OrderedLocusNames=Desru_1295 {ECO:0000313|EMBL:AEG59569.1};
OS Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS (Desulfotomaculum ruminis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG59569.1, ECO:0000313|Proteomes:UP000009234};
RN [1] {ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA Spring S., Klenk H.-P., Woyke T.;
RT "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG59569.1, ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RX PubMed=23408247; DOI=10.4056/sigs.3226659;
RA Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT "Complete genome sequence of the sulfate-reducing firmicute
RT Desulfotomaculum ruminis type strain (DL(T)).";
RL Stand. Genomic Sci. 7:304-319(2012).
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:0000256|ARBA:ARBA00025475,
CC ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000619, ECO:0000256|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:0000256|ARBA:ARBA00005091, ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000256|ARBA:ARBA00011152,
CC ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01013,
CC ECO:0000256|RuleBase:RU003657}.
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DR EMBL; CP002780; AEG59569.1; -; Genomic_DNA.
DR RefSeq; WP_013841340.1; NC_015589.1.
DR AlphaFoldDB; F6DPJ2; -.
DR STRING; 696281.Desru_1295; -.
DR KEGG; dru:Desru_1295; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_9; -.
DR OrthoDB; 9781903at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000009234; 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; Aldolase class I; 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 NCBIfam; TIGR00735; hisF; 1.
DR PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01013};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01013}; Lyase {ECO:0000256|HAMAP-Rule:MF_01013};
KW Reference proteome {ECO:0000313|Proteomes:UP000009234}.
FT ACT_SITE 11
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 252 AA; 27048 MW; DA19745D185BBFA0 CRC64;
MLMKRIIPCL DVTGGRVVKG TNFVNLRDAG DPVELAALYD REGADEVIFL DITASSDGRA
TMLDVVRRTA EEVFIPFTVG GGIRTVEDMR LMLQAGADKI GINTAAIKNP RVISEGALKF
GSQCVVVAID ARQTGPRKWE VYIHGGRTPT GMDAVEWAAK AEELGAGEIL LTSMDRDGTK
EGFDLALTRT IAQAVKIPVI ASGGVGTLEH MAQGLTEGMA DAALAASIFH FGEYSVRQAK
EYLRERGVPV RL
//
