ID M4S1C3_9SPHN Unreviewed; 253 AA.
AC M4S1C3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=G432_10435 {ECO:0000313|EMBL:AGH49810.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH49810.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH49810.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH49810.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
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; CP004036; AGH49810.1; -; Genomic_DNA.
DR RefSeq; WP_015458807.1; NC_020561.1.
DR AlphaFoldDB; M4S1C3; -.
DR STRING; 745310.G432_10435; -.
DR KEGG; sphm:G432_10435; -.
DR PATRIC; fig|745310.14.peg.2173; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_5; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000011816; 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};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01013, ECO:0000313|EMBL:AGH49810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011816}.
FT ACT_SITE 12
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01013"
SQ SEQUENCE 253 AA; 25958 MW; D51AEB564E02D54B CRC64;
MTVRTRIIPC LDVAGGRVVK GVNFVDLADA GDPVEQARVY DAAGADELCF LDITATHEGR
GTILDVVART AAVCFMPLTV GGGVRSADDA RALLLAGADK VAVNSAAVAR PELVAEMAER
FGAQCVVGAV DARAVAPGRW EIFTHGGRKP TGIDAVAHAV RLAELGAGEL LVTSMDRDGT
RDGYDLALTR AIADRVRVPV IASGGVGALD HLVAGVVEGH ASAVLAASIF HFGQHSIAEA
RAALRAAGLP VRA
//
