ID HIS4_ARATH Reviewed; 592 AA.
AC Q9SZ30; O80330; Q8GX14;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Imidazole glycerol phosphate synthase hisHF, chloroplastic;
DE Short=IGP synthase;
DE Short=IGPS;
DE Short=ImGP synthase;
DE EC=4.3.2.10;
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 4;
DE Includes:
DE RecName: Full=Glutaminase;
DE EC=3.5.1.2;
DE Includes:
DE RecName: Full=Cyclase;
DE Flags: Precursor;
GN Name=HISN4; OrderedLocusNames=At4g26900; ORFNames=F10M23.240;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9654139; DOI=10.1016/s0014-5793(98)00535-3;
RA Fujimori K., Ohta D.;
RT "An Arabidopsis cDNA encoding a bifunctional glutamine
RT amidotransferase/cyclase suppresses the histidine auxotrophy of a
RT Saccharomyces cerevisiae his7 mutant.";
RL FEBS Lett. 428:229-234(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
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 -!- 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HisA/HisF family.
CC {ECO:0000305}.
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DR EMBL; AB006210; BAA28783.1; -; mRNA.
DR EMBL; AB016783; BAA32287.1; -; Genomic_DNA.
DR EMBL; AL035440; CAB36536.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79545.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85266.1; -; Genomic_DNA.
DR EMBL; AK118498; BAC43102.1; -; mRNA.
DR EMBL; BT005923; AAO64858.1; -; mRNA.
DR PIR; T04813; T04813.
DR PIR; T48876; T48876.
DR RefSeq; NP_194420.1; NM_118824.4.
DR AlphaFoldDB; Q9SZ30; -.
DR SMR; Q9SZ30; -.
DR BioGRID; 14084; 3.
DR STRING; 3702.Q9SZ30; -.
DR PaxDb; 3702-AT4G26900-1; -.
DR ProteomicsDB; 230396; -.
DR EnsemblPlants; AT4G26900.1; AT4G26900.1; AT4G26900.
DR GeneID; 828797; -.
DR Gramene; AT4G26900.1; AT4G26900.1; AT4G26900.
DR KEGG; ath:AT4G26900; -.
DR Araport; AT4G26900; -.
DR TAIR; AT4G26900; AT-HF.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_037550_0_0_1; -.
DR InParanoid; Q9SZ30; -.
DR OMA; GNYGHFV; -.
DR OrthoDB; 2782495at2759; -.
DR PhylomeDB; Q9SZ30; -.
DR BioCyc; ARA:AT4G26900-MONOMER; -.
DR BioCyc; MetaCyc:AT4G26900-MONOMER; -.
DR BRENDA; 4.3.2.10; 399.
DR UniPathway; UPA00031; UER00010.
DR PRO; PR:Q9SZ30; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ30; baseline and differential.
DR Genevisible; Q9SZ30; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:InterPro.
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; IMP:TAIR.
DR CDD; cd01748; GATase1_IGP_Synthase; 1.
DR CDD; cd04731; HisF; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00735; hisF; 1.
DR NCBIfam; TIGR01855; IMP_synth_hisH; 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; PF00117; GATase; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR PIRSF; PIRSF036936; IGPS_HisHF; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Chloroplast; Glutamine amidotransferase;
KW Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..592
FT /note="Imidazole glycerol phosphate synthase hisHF,
FT chloroplastic"
FT /id="PRO_0000013446"
FT DOMAIN 63..271
FT /note="Glutamine amidotransferase type-1"
FT REGION 280..592
FT /note="Cyclase"
FT ACT_SITE 141
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 246
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 248
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000255"
FT ACT_SITE 447
FT /evidence="ECO:0000255"
FT CONFLICT 110
FT /note="A -> P (in Ref. 1; BAA28783/BAA32287)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> Q (in Ref. 1; BAA28783/BAA32287)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="I -> M (in Ref. 1; BAA28783/BAA32287)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="S -> F (in Ref. 1; BAA28783/BAA32287)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="W -> R (in Ref. 4; AAO64858 and 5; BAC43102)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="R -> Q (in Ref. 1; BAA28783)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="D -> N (in Ref. 1; BAA28783)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..576
FT /note="KTNASAALAAGIFHRKEVPI -> EDKRICRACCRHFPPERGYQS (in
FT Ref. 1; BAA28783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 64192 MW; A8D7F1699C6163CE CRC64;
MEATAAPFSS IVSSRQNFSS SSSIRASSPA SLFLSQKSIG NVNRKFKSPR SLSVRASSTS
DSVVTLLDYG AGNVRSIRNA LRHLGFSIKD VQTPGDILNA DRLIFPGVGA FAPAMDVLNR
TGMAEALCKY IENDRPFLGI CLGLQLLFDS SEENGPVKGL GVIPGIVGRF DASAGIRVPH
IGWNALQVGK DSEILDDVGN RHVYFVHSYR AIPSDENKDW ISSTCNYGES FISSIRRGNV
HAVQFHPEKS GEVGLSVLRR FLHPKLPATQ KPMEGKASKL AKRVIACLDV RTNDKGDLVV
TKGDQYDVRE QSNENEVRNL GKPVDLAGQY YKDGADEISF LNITGFRDFP LGDLPMIQVL
RQTSKNVFVP LTVGGGIRDF TDASGRYYSS LEVAAEYFRS GADKISIGSD AVSAAEEFIK
SGVKTGKSSL EQISRVYGNQ AVVVSIDPRR VYVNHPDDVP YKVIRVTNPG PNGEEYAWYQ
CTVSGGREGR PIGAFELAKA VEELGAGEIL LNCIDCDGQG KGFDIDLVKL ISDSVGIPVI
ASSGAGTPDH FSEVFEKTNA SAALAAGIFH RKEVPIQSVK EHLQEERIEV RI
//
