ID HIS4_PAEAT Reviewed; 247 AA. AC A1R562; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; DE EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014}; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; GN Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014}; GN OrderedLocusNames=AAur_1608; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=290340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter RT aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). 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 Evidence={ECO:0000255|HAMAP-Rule:MF_01014}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP- CC Rule:MF_01014}. 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; CP000474; ABM09313.1; -; Genomic_DNA. DR RefSeq; WP_011774319.1; NC_008711.1. DR PDB; 4WD0; X-ray; 1.50 A; A=1-247. DR PDBsum; 4WD0; -. DR AlphaFoldDB; A1R562; -. DR SMR; A1R562; -. DR STRING; 290340.AAur_1608; -. DR KEGG; aau:AAur_1608; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_1_11; -. DR OrthoDB; 9807749at2; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000637; Chromosome. 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-UniRule. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro. DR CDD; cd04732; HisA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR010188; HisA/PriA_Actinobacteria. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR01919; hisA-trpF; 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; KW Isomerase. FT CHAIN 1..247 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000290447" FT ACT_SITE 16 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT STRAND 10..18 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 21..25 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 39..48 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 59..62 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 69..78 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 80..88 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 92..100 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 110..114 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 130..137 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 207..214 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 215..219 FT /evidence="ECO:0007829|PDB:4WD0" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 228..231 FT /evidence="ECO:0007829|PDB:4WD0" FT HELIX 237..244 FT /evidence="ECO:0007829|PDB:4WD0" SQ SEQUENCE 247 AA; 26175 MW; A0839617E7505388 CRC64; MTTSAQSVLE LLPAVDIVDG QAVRLLQGEA GSETSYGTPL EAALNWQNDG AEWVHMVDLD AAFGRGNNAA LISDVVSQLN VKVELSGGLR DDESLERALE LGVARVNLGT AALENPEWTR KAIDRFGDKI AVGLDVRGTT LAGRGWTKEG GDLWEVLARL EDAGCARYVV TDVTKDGTLQ GPNVELLRQM VEKTGKPVVA SGGISSLEDL RVLRELVPLG VEGAIVGKAL YAGAFTLPEA LDVAGRR //