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   04-NOV-2026, entry version 190.
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; DOI=10.1038/387s084;
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.
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   AlphaFoldDB; P40545; -.
DR   SMR; P40545; -.
DR   BioGRID; 34968; 26.
DR   DIP; DIP-4716N; -.
DR   FunCoup; P40545; 309.
DR   IntAct; P40545; 2.
DR   STRING; 4932.YIL020C; -.
DR   iPTMnet; P40545; -.
DR   PaxDb; 4932-YIL020C; -.
DR   PeptideAtlas; P40545; -.
DR   EnsemblFungi; YIL020C_mRNA; YIL020C; YIL020C.
DR   GeneID; 854792; -.
DR   KEGG; sce:YIL020C; -.
DR   AGR; SGD:S000001282; -.
DR   SGD; S000001282; HIS6.
DR   VEuPathDB; FungiDB:YIL020C; -.
DR   eggNOG; KOG3055; Eukaryota.
DR   HOGENOM; CLU_065050_0_0_1; -.
DR   InParanoid; P40545; -.
DR   OMA; AAINKWQ; -.
DR   OrthoDB; 446074at2759; -.
DR   BioCyc; YEAST:YIL020C-MONOMER; -.
DR   BRENDA; 5.3.1.16; 984.
DR   UniPathway; UPA00031; UER00009.
DR   BioGRID-ORCS; 854792; 1 hit in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
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:L-histidine biosynthetic process; IMP:SGD.
DR   CDD; cd04723; HisA_HisF; 1.
DR   FunFam; 3.20.20.70:FF:000110; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011858; His6/HISN3.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR02129; hisA_euk; 1.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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           219..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
//