ID HIS4_YARLI Reviewed; 264 AA. AC Q6C2U0; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 100. 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; OrderedLocusNames=YALI0F05192g; OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=284591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR382132; CAG77829.1; -; Genomic_DNA. DR RefSeq; XP_505022.1; XM_505022.1. DR AlphaFoldDB; Q6C2U0; -. DR SMR; Q6C2U0; -. DR STRING; 284591.Q6C2U0; -. DR EnsemblFungi; CAG77829; CAG77829; YALI0_F05192g. DR GeneID; 2908162; -. DR KEGG; yli:YALI0F05192g; -. DR VEuPathDB; FungiDB:YALI0_F05192g; -. DR HOGENOM; CLU_065050_0_0_1; -. DR InParanoid; Q6C2U0; -. DR OMA; IEWNKTH; -. DR OrthoDB; 312953at2759; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000001300; Chromosome F. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR CDD; cd04723; HisA_HisF; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 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 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase; KW Reference proteome. FT CHAIN 1..264 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000141962" SQ SEQUENCE 264 AA; 29098 MW; 1FAA1398C238C79A CRC64; MTKFRGCIDI HSGQVKQIVG GTLTDSDADL KTNFVATQPP GYFAQLYKDN NVVGTHVIKL GPGCDEAAEE ALAGWPDHLQ IGGGINHDNA EKWIKLGASH VIVTSFLFPD AKLDMKRLTD LEAILEPYGG KKRIVVDLSC RRKDGKWVVA MNRWQTLTDT EVNKETLEQL AKHCDEFLIH AADVEGLCNG IDEELVTKLG EWLEEGHLPP VTYAGGAKNI DDLALVQKLS HGKVDLTYGS ALDVFGGDKV KFSDCVEWNE KMHK //