HIS4_CANGA
ID HIS4_CANGA Reviewed; 261 AA.
AC Q6FPN5;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=CAGL0J02398g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR EMBL; CR380956; CAG60758.1; -; Genomic_DNA.
DR RefSeq; XP_447809.1; XM_447809.1.
DR AlphaFoldDB; Q6FPN5; -.
DR SMR; Q6FPN5; -.
DR STRING; 5478.XP_447809.1; -.
DR PRIDE; Q6FPN5; -.
DR EnsemblFungi; CAG60758; CAG60758; CAGL0J02398g.
DR GeneID; 2889762; -.
DR KEGG; cgr:CAGL0J02398g; -.
DR CGD; CAL0133580; CAGL0J02398g.
DR VEuPathDB; FungiDB:CAGL0J02398g; -.
DR eggNOG; KOG3055; Eukaryota.
DR HOGENOM; CLU_065050_0_0_1; -.
DR InParanoid; Q6FPN5; -.
DR OMA; MTKFRPC; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000002428; Chromosome J.
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;
KW Reference proteome.
FT CHAIN 1..261
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000141957"
SQ SEQUENCE 261 AA; 29191 MW; B1A088D2BC57D326 CRC64;
MTKFVGCIDL HDGQVKQIVG GTLKDNDDSL ETNFVSKYPP SYYAQLYLEN RIEGCHVIKL
GPNNDAAAME ALNAAPGFLQ VGGGINDENC LQWLEKASKI IVTSWLFTKE GTFLMDRLQL
LSNKCGPDRI VVDLSCRRTP DSKWVVAMNK WQTLTTLELN KETFTELSKY TDEFLIHAAD
VEGLCKGIET DLVTKLYEWT KDINKEVKIV YAGGAKSISD LELVDKLSNG TVDLTYGSSL
DIFGGKLVRF QDCCEWNSKH N