HIS6_CERS4
ID HIS6_CERS4 Reviewed; 253 AA.
AC P50937; Q3J487;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 114.
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=RHOS4_08290; ORFNames=RSP_2242;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Oriol E.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; X87256; CAA60710.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA78397.1; -; Genomic_DNA.
DR PIR; S54838; S54838.
DR RefSeq; WP_009562844.1; NZ_CP030271.1.
DR RefSeq; YP_352298.1; NC_007493.2.
DR AlphaFoldDB; P50937; -.
DR SMR; P50937; -.
DR STRING; 272943.RSP_2242; -.
DR EnsemblBacteria; ABA78397; ABA78397; RSP_2242.
DR KEGG; rsp:RSP_2242; -.
DR PATRIC; fig|272943.9.peg.1145; -.
DR eggNOG; COG0107; Bacteria.
DR OMA; IFHYKET; -.
DR PhylomeDB; P50937; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002703; Chromosome 1.
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..253
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142219"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="G -> A (in Ref. 1; CAA60710)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..121
FT /note="AEAADRFG -> PSRRPLR (in Ref. 1; CAA60710)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="A -> T (in Ref. 1; CAA60710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 26243 MW; A1F47ABC71C62054 CRC64;
MLKTRIIPCL DVADGRVVKG VNFVDLRDAG DPVEAARAYD AAGADELCFL DIHATHENRG
TMYDLVTRTA EQCFMPLTVG GGVRTHQDVR ALLLAGADKV SFNSAAVADP GVVAEAADRF
GSQCIVVAID AKTVAPGRWE IFTHGGRRAT GIDAVAFACE MASRGAGEIL LTSMDRDGTR
AGFNLPLTRA ISDAVPIPVI ASGGVGTLDH LVEGVTEGGA SAVLAASIFH FGEFTIGEAK
AHMAAAGIPV RLA
