HIS5_EMENI
ID HIS5_EMENI Reviewed; 553 AA.
AC Q9P4P9; C8VBA3; Q5AWA0;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 135.
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=hisHF; ORFNames=AN7430;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A234;
RX PubMed=11277623; DOI=10.1006/fgbi.2000.1244;
RA Valerius O., Draht O., Kuebler E., Adler K., Hoffmann B., Braus G.H.;
RT "Regulation of hisHF transcription of Aspergillus nidulans by adenine and
RT amino acid limitation.";
RL Fungal Genet. Biol. 32:21-31(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF159463; AAF80376.1; -; Genomic_DNA.
DR EMBL; AACD01000129; EAA62010.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF79365.1; -; Genomic_DNA.
DR RefSeq; XP_680699.1; XM_675607.1.
DR AlphaFoldDB; Q9P4P9; -.
DR SMR; Q9P4P9; -.
DR STRING; 162425.CADANIAP00000520; -.
DR PRIDE; Q9P4P9; -.
DR EnsemblFungi; CBF79365; CBF79365; ANIA_07430.
DR EnsemblFungi; EAA62010; EAA62010; AN7430.2.
DR GeneID; 2869606; -.
DR KEGG; ani:AN7430.2; -.
DR VEuPathDB; FungiDB:AN7430; -.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_037550_0_0_1; -.
DR InParanoid; Q9P4P9; -.
DR OMA; GHFGHCM; -.
DR OrthoDB; 365987at2759; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central.
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; IEA:UniProtKB-UniPathway.
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..553
FT /note="Imidazole glycerol phosphate synthase hisHF"
FT /id="PRO_0000152474"
FT DOMAIN 3..223
FT /note="Glutamine amidotransferase type-1"
FT REGION 232..553
FT /note="Cyclase"
FT ACT_SITE 81
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /evidence="ECO:0000255"
FT ACT_SITE 403
FT /evidence="ECO:0000255"
FT CONFLICT 171..173
FT /note="TAS -> RRV (in Ref. 1; AAF80376)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..221
FT /note="AGLRTLRAFLDGAQLHSVTLE -> GRPTHPSRFLGRSSAPFCHIR (in
FT Ref. 1; AAF80376)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..489
FT /note="FDLELINHVKA -> SILTDQPPSKR (in Ref. 1; AAF80376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 60153 MW; EB1D9681269B7D28 CRC64;
MPTVHLLDYV AGNVRSLVNA INKVGYEVEW VRSPSDLKDV EKLILPGVGH FGHCLSQLSS
GGYLQPIREH IASGKPFMGI CVGLQSLFES SEEDPNIPGL GTIPARLRKF DAKTKSVPHI
GWNSATDTRI DSTGGQTFYG LSPSSKYYYV HSYAAPYEPG ILEKDGWLVA TASYGEEKFI
GAIARDNIFA TQFHPEKSGQ AGLRTLRAFL DGAQLHSVTL EDSILTGEKN GLTRRIIACL
DVRTNDVGDL VVTKGDQYDV REKDGADAGG QVRNLGKPVD MAKKYYEQGA DEVTFLNITS
FRNCPLADLP MLEILRRTSE TVFVPLTIGG GIRDTVDTDG THIPALDVAS MYFKSGADKV
SIGSDAVVAA EDYYAAGKVL SGKTAIETIS KAYGNQAVVV SVDPKRVYVS QPEDTKHRTI
ETKFPNAAGQ NFCWYQCTIK GGRETRDLDV CQLVQAVEAM GAGEILLNCI DKDGSNSGFD
LELINHVKAA VKIPVIASSG AGMPKHFEEV FDQTTTDAAL GAGMFHRGEY TVGEVKQYLE
DRGFLVRRFE PDV
