HIS5_SCHPO
ID HIS5_SCHPO Reviewed; 541 AA.
AC O94303; Q9Y7X3;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Imidazole glycerol phosphate synthase hisHF;
DE Short=IGP synthase;
DE Short=IGPS;
DE Short=ImGP synthase;
DE EC=4.3.2.10;
DE Includes:
DE RecName: Full=Glutaminase;
DE EC=3.5.1.2;
DE Includes:
DE RecName: Full=Cyclase;
GN Name=his4; ORFNames=SPBC418.01c, SPBC887.20c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC AICAR and glutamate. The glutaminase domain produces the ammonia
CC necessary for the cyclase domain to produce IGP and AICAR from PRFAR.
CC The ammonia is channeled to the active site of the cyclase domain.
CC {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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HisA/HisF family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21905.2; -; Genomic_DNA.
DR PIR; T40745; T40745.
DR RefSeq; NP_596494.2; NM_001022414.2.
DR AlphaFoldDB; O94303; -.
DR SMR; O94303; -.
DR BioGRID; 277738; 2.
DR STRING; 4896.SPBC418.01c.1; -.
DR MaxQB; O94303; -.
DR PaxDb; O94303; -.
DR PRIDE; O94303; -.
DR EnsemblFungi; SPBC418.01c.1; SPBC418.01c.1:pep; SPBC418.01c.
DR GeneID; 2541224; -.
DR KEGG; spo:SPBC418.01c; -.
DR PomBase; SPBC418.01c; his4.
DR VEuPathDB; FungiDB:SPBC418.01c; -.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_037550_0_0_1; -.
DR InParanoid; O94303; -.
DR OMA; GHFGHCM; -.
DR PhylomeDB; O94303; -.
DR UniPathway; UPA00031; UER00010.
DR PRO; PR:O94303; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; ISO:PomBase.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; ISO:PomBase.
DR CDD; cd01748; GATase1_IGP_Synthase; 1.
DR CDD; cd04731; HisF; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00278; HisH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR004651; HisF.
DR InterPro; IPR014640; IGPS_HisHF.
DR InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR PIRSF; PIRSF036936; IGPS_HisHF; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00735; hisF; 1.
DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Glutamine amidotransferase;
KW Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme;
KW Reference proteome.
FT CHAIN 1..541
FT /note="Imidazole glycerol phosphate synthase hisHF"
FT /id="PRO_0000152475"
FT DOMAIN 2..214
FT /note="Glutamine amidotransferase type-1"
FT REGION 228..541
FT /note="Cyclase"
FT ACT_SITE 80
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 237
FT /evidence="ECO:0000255"
FT ACT_SITE 396
FT /evidence="ECO:0000255"
SQ SEQUENCE 541 AA; 59400 MW; DFF1DC3102141C74 CRC64;
MIVSIVDYGS GNVRSLINAV RYLGFETQWI RNPHDIEKAE CLIFPGVGNF GFVCDSLAKQ
GFLEPLRRYA LSGKPFMAVC VGIQALFEGS VEAPHSKGLG VFPGLVQRFD NDDKTVPHIG
WNSCAVRSDT SKEFFGMRPH DKFYFVHSYM IPEKGLILPP EFKIATTKYG NETFVGAIVK
NNFLATQFHP EKSGSAGLRC LKAFLTGNYE QPISGEASKL IENSFGGLTK RIIACLDVRS
NDAGDLVVTK GDQYDVREKS SGSEVRNLGK PVELCQRYFQ EGADEVVFLN ITSFRNCPMA
DAPMLQVLEK AAQTVFVPLT VGGGIRDVSD PDGTFHPAVE VAGIYFRSGA DKVSIGSDAV
YAAEKYYENG KKLSGKTAIE TISKAYGNQA VVISVDPKRQ YVKVPEDTKH HVVKTSRLGP
NGEAYCWYQC TVKGGREYRD IDVVELTRAC EAMGAGEVLL NCMDQDGSNA GYDIELVRLV
KNSVNIPVIA SSGAGIPQHF EEVFKETDCD AALAAGIFHR QTCRIEDVKE YLAIHDVLVR
T
