ID HIS4_SCHPO Reviewed; 264 AA. AC Q10184; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 134. 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 ORFNames=SPAC3F10.09; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). 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; CU329670; CAA93307.1; -; Genomic_DNA. DR PIR; T38710; T38710. DR RefSeq; NP_593941.1; NM_001019369.2. DR AlphaFoldDB; Q10184; -. DR SMR; Q10184; -. DR BioGRID; 279535; 14. DR STRING; 284812.Q10184; -. DR MaxQB; Q10184; -. DR PaxDb; 4896-SPAC3F10-09-1; -. DR EnsemblFungi; SPAC3F10.09.1; SPAC3F10.09.1:pep; SPAC3F10.09. DR GeneID; 2543103; -. DR KEGG; spo:SPAC3F10.09; -. DR PomBase; SPAC3F10.09; -. DR VEuPathDB; FungiDB:SPAC3F10.09; -. DR eggNOG; KOG3055; Eukaryota. DR HOGENOM; CLU_065050_0_0_1; -. DR InParanoid; Q10184; -. DR OMA; IEWNKTH; -. DR PhylomeDB; Q10184; -. DR UniPathway; UPA00031; UER00009. DR PRO; PR:Q10184; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. 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_0000141961" SQ SEQUENCE 264 AA; 29346 MW; 8C97F79938BDEB60 CRC64; MEKSQHTLFR PCIDIHQGQV KQIVGGTLGN DADVKTNYVS LKPSSYYAEL YKLNHLEGAH VIMLGPNCEE AAKTALHTWP GALQIGGGIN ISNAQNWLQE GASKVIVTSW LFPDAQFDLD RLKAISSKIG KDRLVVDVSC RRKDNRWFAA INKWQVMTAF ELNEENLDLL SQYCSEFLIH AADVEGLCKG IDEDLVIKLG EWVKIPTTYA GGGRSIEDLD LVDKLSKGKV DLTIGSALDI FGGVLEFTRV VAWNRRFTPL PLQD //