ID HIS4_DEBHA Reviewed; 276 AA. AC Q6BUV9; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 27-MAR-2024, entry version 101. 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=DEHA2C07568g; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC RC 2968; 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; CR382135; CAG86070.2; -; Genomic_DNA. DR RefSeq; XP_458010.2; XM_458010.1. DR AlphaFoldDB; Q6BUV9; -. DR SMR; Q6BUV9; -. DR STRING; 284592.Q6BUV9; -. DR GeneID; 2900784; -. DR KEGG; dha:DEHA2C07568g; -. DR VEuPathDB; FungiDB:DEHA2C07568g; -. DR eggNOG; KOG3055; Eukaryota. DR HOGENOM; CLU_065050_0_0_1; -. DR InParanoid; Q6BUV9; -. DR OMA; IEWNKTH; -. DR OrthoDB; 312953at2759; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000599; Chromosome C. 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 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..276 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000141958" SQ SEQUENCE 276 AA; 30521 MW; 1D02F6F017793872 CRC64; MTKFRGCIDI HSGQVKQIVG GTLTQDDTTE LNHKSTTTEN FVSTKPSSYY AELYKNAGIN GCHVIKLGSN PENDEAAKLA CQSWPNNLQV GGGINGDNAL EWLDVHKASH VILTSWLFSD SDEGKEFDWV KLKRVSELVG KSRLIVDLSC RELRVDDKIE WVVAMNKWQT LTNNKLSAEF LGEVSQYCDE FLIHAADVEG LCNGIDVNLV AKLGEWCPEG FEGKIVYAGG ARSVKDLDTV SKLSDDKVDL TYGSALDVFG GKLVKFDDLV SWNELH //