HIS2_YEAST
ID HIS2_YEAST Reviewed; 799 AA.
AC P00815; D6VQY5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Histidine biosynthesis trifunctional protein {ECO:0000305};
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE EC=3.5.4.19 {ECO:0000250|UniProtKB:Q50837};
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE EC=3.6.1.31 {ECO:0000250|UniProtKB:O82768};
DE Includes:
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23 {ECO:0000250|UniProtKB:P9WNW9};
GN Name=HIS4 {ECO:0000303|PubMed:7049842, ECO:0000312|SGD:S000000535};
GN OrderedLocusNames=YCL030C; ORFNames=YCL183, YCL30C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7049842; DOI=10.1016/0378-1119(82)90055-5;
RA Donahue T.F., Farabaugh P.J., Fink G.R.;
RT "The nucleotide sequence of the HIS4 region of yeast.";
RL Gene 18:47-59(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1897318; DOI=10.1002/yea.320070513;
RA Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT encompasses four new open reading frames.";
RL Yeast 7:533-538(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION TO 375.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-20.
RX PubMed=6250062; DOI=10.1038/286352a0;
RA Farabaugh P.J., Fink G.R.;
RT "Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair
RT duplication.";
RL Nature 286:352-356(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=2991923; DOI=10.1073/pnas.82.16.5428;
RA Roeder G.S., Rose A.B., Pearlman R.E.;
RT "Transposable element sequences involved in the enhancement of yeast gene
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5428-5432(1985).
RN [8]
RP INDUCTION.
RX PubMed=8336737; DOI=10.1128/mcb.13.8.5099-5111.1993;
RA Rolfes R.J., Hinnebusch A.G.;
RT "Translation of the yeast transcriptional activator GCN4 is stimulated by
RT purine limitation: implications for activation of the protein kinase
RT GCN2.";
RL Mol. Cell. Biol. 13:5099-5111(1993).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC Evidence={ECO:0000250|UniProtKB:Q50837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000250|UniProtKB:O82768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC ChEBI:CHEBI:57945; EC=1.1.1.23;
CC Evidence={ECO:0000250|UniProtKB:P9WNW9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P9WNW9};
CC Note=Binds 1 zinc ion. {ECO:0000250|UniProtKB:P9WNW9};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- INTERACTION:
CC P00815; P53233: FMP48; NbExp=3; IntAct=EBI-8334, EBI-9664;
CC -!- INDUCTION: Induced by amino acid and purine starvation in a GCN4
CC dependent manner. {ECO:0000269|PubMed:8336737}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; V01310; CAA24617.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42355.2; -; Genomic_DNA.
DR EMBL; V01309; CAA24616.1; -; Genomic_DNA.
DR EMBL; M11491; AAA67504.1; -; Genomic_DNA.
DR EMBL; M11492; AAA67505.1; -; Genomic_DNA.
DR EMBL; M11694; AAA18400.1; -; Unassigned_DNA.
DR EMBL; M11695; AAA18401.1; -; Unassigned_DNA.
DR EMBL; M11696; AAA18402.1; -; Unassigned_DNA.
DR EMBL; BK006937; DAA07454.1; -; Genomic_DNA.
DR PIR; S17473; SHBY.
DR RefSeq; NP_009900.2; NM_001178675.1.
DR AlphaFoldDB; P00815; -.
DR SMR; P00815; -.
DR BioGRID; 30953; 33.
DR DIP; DIP-6402N; -.
DR IntAct; P00815; 14.
DR MINT; P00815; -.
DR STRING; 4932.YCL030C; -.
DR iPTMnet; P00815; -.
DR MaxQB; P00815; -.
DR PaxDb; P00815; -.
DR PRIDE; P00815; -.
DR EnsemblFungi; YCL030C_mRNA; YCL030C; YCL030C.
DR GeneID; 850327; -.
DR KEGG; sce:YCL030C; -.
DR SGD; S000000535; HIS4.
DR VEuPathDB; FungiDB:YCL030C; -.
DR eggNOG; KOG2697; Eukaryota.
DR eggNOG; KOG4311; Eukaryota.
DR HOGENOM; CLU_006732_0_1_1; -.
DR InParanoid; P00815; -.
DR OMA; WEAADLF; -.
DR BioCyc; YEAST:YCL030C-MON; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR UniPathway; UPA00031; UER00014.
DR PRO; PR:P00815; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P00815; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IDA:SGD.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IDA:SGD.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:SGD.
DR CDD; cd06572; Histidinol_dh; 1.
DR Gene3D; 3.10.20.810; -; 1.
DR HAMAP; MF_01024; HisD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR016298; Histidine_synth_trifunct.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR012131; Hstdl_DH.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR PIRSF; PIRSF001257; His_trifunctional; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF141734; SSF141734; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis; Hydrolase;
KW Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..799
FT /note="Histidine biosynthesis trifunctional protein"
FT /id="PRO_0000135914"
FT REGION 1..229
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000250|UniProtKB:O82768"
FT REGION 230..312
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT /evidence="ECO:0000250|UniProtKB:O82768"
FT REGION 313..799
FT /note="Histidinol dehydrogenase"
FT /evidence="ECO:0000250|UniProtKB:P9WNW9"
FT ACT_SITE 687
FT /evidence="ECO:0000250"
FT ACT_SITE 688
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="A -> R (in Ref. 1; CAA24617)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="H -> Y (in Ref. 1; CAA24617)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..403
FT /note="AL -> VF (in Ref. 1; CAA24617)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> N (in Ref. 1; CAA24617)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="I -> F (in Ref. 1; CAA24617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 87721 MW; 0B82D289BEAB754D CRC64;
MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP LVALSLPSGK
FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER VVVEENGVFS NQFMVKQKFS
QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL
GRGVYYSRSR NEIWIKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE
FKHGLVGLES LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA
DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE EKLTGPIHLD
VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN SALLEYTEKF DGVKLSNPVL
NAPFPEEYFE GLTEEMKEAL DLSIENVRKF HAAQLPTETL EVETQPGVLC SRFPRPIEKV
GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGASKIV
LAGGAQAVAA MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV
IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA LQLPRVDIVR
KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG
DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH
RNAVKIRMSK LGLIPKDFQ
