ID HIS4_OPITP Reviewed; 243 AA. AC B1ZW12; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Oter_2745; OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1). OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus. OX NCBI_TaxID=452637; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11246 / JCM 15787 / PB90-1; RX PubMed=21398538; DOI=10.1128/jb.00228-11; RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A., RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J., RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N., RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.; RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an RT abundant inhabitant of rice paddy soil ecosystems."; RL J. Bacteriol. 193:2367-2368(2011). 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; CP001032; ACB76026.1; -; Genomic_DNA. DR RefSeq; WP_012375561.1; NC_010571.1. DR AlphaFoldDB; B1ZW12; -. DR SMR; B1ZW12; -. DR STRING; 452637.Oter_2745; -. DR KEGG; ote:Oter_2745; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_1_0; -. DR OrthoDB; 9781704at2; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000007013; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. 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; IPR006063; HisA_bact_arch. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 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..243 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_1000213231" FT ACT_SITE 8 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 128 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" SQ SEQUENCE 243 AA; 25360 MW; 43C0AA8B1C4959D8 CRC64; MTIYPAIDIK GGRCVRLTQG RAEQETIYAQ NPADVAMQFR AAGSEWVHVV DLDGAFAGEP QNLAAVQAIV AVGMKVQFGG GLRTRAAVER ALALGVSRVV LGTRAAESES FVGELVQAFG DKIAVGIDAK NGKVAVKGWV ATADLSTLVL ARRMDTLGVA TLIHTDIGTD GMLTGPNLAA QEALCSAVKS RVIASGGVSR RDDVVNLAKL AQRHANLDGV IVGKALYERR VELADLLSLA AAS //