ID   HIS4_CANAX              Reviewed;         279 AA.
AC   Q9HFV5;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE            EC=5.3.1.16;
DE   AltName: Full=5-proFAR isomerase;
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN   Name=HIS6;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Day T.W., Davisson V.J.;
RT   "Cloning and characterization of the CaHIS6 and CaHIS7 genes from the
RT   fungal pathogen Candida albicans.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:0000250}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR   EMBL; AF290199; AAG17873.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HFV5; -.
DR   SMR; Q9HFV5; -.
DR   CGD; CAL0000175514; orf19.8833.
DR   VEuPathDB; FungiDB:C4_05640C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03258; -.
DR   UniPathway; UPA00031; UER00009.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase.
FT   CHAIN           1..279
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000141956"
SQ   SEQUENCE   279 AA;  30796 MW;  259D1E50F41C4624 CRC64;
     MTKFRGCIDI HSGQVKQIVG GTLTQDDSAS SKTSSAKENF VSTKPSSHYA QLYKDYNVKG
     CHVIKLGSNP ANDDAAKLAL STWPHNLQVG GGINLDNAQY WLDQGASHVI LTSWLFTKNE
     QDKMELDFGK LREISKLIGK EKLIVDLSCR TVIENGKTNW YVAMNKWQTI TDTILSAEFL
     LKVSAYCDEF LIHAADVEGL CKGIDEKLVE NLGEWCPVGF EEKIVYAGGA KSINDLDTVA
     KLSKGKVDLT YGSSLDIFSG KLVNFTDLVE WNKANSKTN