HIS6_RHOCB
ID HIS6_RHOCB Reviewed; 253 AA.
AC O30724; D5ARP0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 105.
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=RCAP_rcc01153;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MT1131;
RX PubMed=9473054; DOI=10.1128/jb.180.4.969-978.1998;
RA Koch H.G., Hwang O., Daldal F.;
RT "Isolation and characterization of Rhodobacter capsulatus mutants affected
RT in cytochrome cbb3 oxidase activity.";
RL J. Bacteriol. 180:969-978(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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; AF016223; AAC46105.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84911.1; -; Genomic_DNA.
DR RefSeq; WP_013066890.1; NC_014034.1.
DR AlphaFoldDB; O30724; -.
DR SMR; O30724; -.
DR STRING; 272942.RCAP_rcc01153; -.
DR EnsemblBacteria; ADE84911; ADE84911; RCAP_rcc01153.
DR GeneID; 31490066; -.
DR KEGG; rcp:RCAP_rcc01153; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_5; -.
DR OMA; IFHYKET; -.
DR OrthoDB; 1522718at2; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000002361; 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..253
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142218"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT CONFLICT 114..121
FT /note="AEAADRFG -> RSRRSLR (in Ref. 1; AAC46105)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> P (in Ref. 1; AAC46105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 26438 MW; 9D2870580BC68556 CRC64;
MLKTRIIPCL DVADGRVVKG VNFVNLIDAG DPVEAAKAYD AAGADELCFL DIHATHENRG
TMFDLVTRTA EQCFMPLTVG GGVRTQEDVR ALLLAGADKV SFNSAAVANP DVVAEAADRF
GSQCIVVAID AKTVEPGRWE IFTHGGRKST GIDAVEFARH VEAKGAGEIL LTSMDRDGTK
AGFNLPLTRA IADAVKIPVI ASGGVGTLDH LVEGVTEGHA SAVLAASIFH FGTYTIGEAK
AHMAAAGIPM RLA
