ID HIS4_PYRAE Reviewed; 229 AA. AC Q8ZY14; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=PAE0991; OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP OS 104966 / NBRC 100827 / IM2). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=178306; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / RC IM2; RX PubMed=11792869; DOI=10.1073/pnas.241636498; RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., RA Miller J.H.; RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum RT aerophilum."; RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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; AE009441; AAL63182.1; -; Genomic_DNA. DR AlphaFoldDB; Q8ZY14; -. DR SMR; Q8ZY14; -. DR STRING; 178306.PAE0991; -. DR EnsemblBacteria; AAL63182; AAL63182; PAE0991. DR KEGG; pai:PAE0991; -. DR PATRIC; fig|178306.9.peg.737; -. DR eggNOG; arCOG00618; Archaea. DR HOGENOM; CLU_048577_1_1_2; -. DR InParanoid; Q8ZY14; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000002439; Chromosome. 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; cd04732; HisA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. 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..229 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000142100" FT ACT_SITE 7 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 124 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 229 AA; 24831 MW; F064FDBEC3B0B7FA CRC64; MIIPSIDIEG GRAVKRIRGQ RGNYIFQGDP LELAARFRKA PLVHVVDLDG AEAGGLVNIS VISKIAEILE GRCELGGGLR SLEAVERALS LCQYAVVGSL PFKNWPLFRR AAELYRDRLA VSLDYRGGEV LVGGWREKAA SIAEAVRRLE EAGPYAAVIV TSVEVEGTGG GVKADIDVKS LKRIARRVFY AGGVRDCNDV ERAYALGFDG VIVGYALYAG DLKKCANWY //