HIS4_YEAST
ID HIS4_YEAST Reviewed; 261 AA.
AC P40545; D6VVQ9; Q6Q5P5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000303|PubMed:9332345};
DE EC=5.3.1.16 {ECO:0000305|PubMed:9332345};
DE AltName: Full=5-proFAR isomerase {ECO:0000303|PubMed:9332345};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000303|PubMed:9332345};
GN Name=HIS6 {ECO:0000303|PubMed:9332345}; OrderedLocusNames=YIL020C;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=YNN 282;
RX PubMed=9332345; DOI=10.1016/s0378-1119(97)00146-7;
RA Fani R., Tamburini E., Mori E., Lazcano A., Lio P., Barberio C.,
RA Casalone E., Cavalieri D., Perito B., Polsinelli M.;
RT "Paralogous histidine biosynthetic genes: evolutionary analysis of the
RT Saccharomyces cerevisiae HIS6 and HIS7 genes.";
RL Gene 197:9-17(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 2-261.
RX PubMed=16731983; DOI=10.1110/ps.062144406;
RA Quevillon-Cheruel S., Leulliot N., Graille M., Blondeau K., Janin J.,
RA van Tilbeurgh H.;
RT "Crystal structure of the yeast His6 enzyme suggests a reaction
RT mechanism.";
RL Protein Sci. 15:1516-1521(2006).
CC -!- FUNCTION: Catalyzes the isomerization of the aminoaldose moiety of
CC ProFAR to the aminoketose of PRFAR. {ECO:0000305|PubMed:9332345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC Evidence={ECO:0000305|PubMed:9332345};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 6490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; X87341; CAA60779.1; -; Genomic_DNA.
DR EMBL; Z46881; CAA86972.1; -; Genomic_DNA.
DR EMBL; AY557859; AAS56185.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08525.1; -; Genomic_DNA.
DR PIR; S49962; S49962.
DR RefSeq; NP_012244.3; NM_001179370.3.
DR PDB; 2AGK; X-ray; 1.30 A; A=2-261.
DR PDBsum; 2AGK; -.
DR AlphaFoldDB; P40545; -.
DR SMR; P40545; -.
DR BioGRID; 34968; 21.
DR DIP; DIP-4716N; -.
DR IntAct; P40545; 1.
DR MINT; P40545; -.
DR STRING; 4932.YIL020C; -.
DR MaxQB; P40545; -.
DR PaxDb; P40545; -.
DR PRIDE; P40545; -.
DR EnsemblFungi; YIL020C_mRNA; YIL020C; YIL020C.
DR GeneID; 854792; -.
DR KEGG; sce:YIL020C; -.
DR SGD; S000001282; HIS6.
DR VEuPathDB; FungiDB:YIL020C; -.
DR eggNOG; KOG3055; Eukaryota.
DR HOGENOM; CLU_065050_0_0_1; -.
DR InParanoid; P40545; -.
DR OMA; MTKFRPC; -.
DR BioCyc; YEAST:YIL020C-MON; -.
DR BRENDA; 5.3.1.16; 984.
DR UniPathway; UPA00031; UER00009.
DR EvolutionaryTrace; P40545; -.
DR PRO; PR:P40545; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40545; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IGI:SGD.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:SGD.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011858; His6-like_euk.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02129; hisA_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Isomerase; Reference proteome.
FT CHAIN 1..261
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000141963"
FT CONFLICT 243
FT /note="F -> S (in Ref. 4; AAS56185)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2AGK"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:2AGK"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2AGK"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2AGK"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2AGK"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2AGK"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2AGK"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:2AGK"
SQ SEQUENCE 261 AA; 29557 MW; FA33F3A8ED52B526 CRC64;
MTKFIGCIDL HNGEVKQIVG GTLTSKKEDV PKTNFVSQHP SSYYAKLYKD RDVQGCHVIK
LGPNNDDAAR EALQESPQFL QVGGGINDTN CLEWLKWASK VIVTSWLFTK EGHFQLKRLE
RLTELCGKDR IVVDLSCRKT QDGRWIVAMN KWQTLTDLEL NADTFRELRK YTNEFLIHAA
DVEGLCGGID ELLVSKLFEW TKDYDDLKIV YAGGAKSVDD LKLVDELSHG KVDLTFGSSL
DIFGGNLVKF EDCCRWNEKQ G
