ID HIS4_CALS8 Reviewed; 237 AA. AC A4XL21; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=Csac_2021; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T OS 6331). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=351627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., RA Kengen S.M.W., Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000679; ABP67606.1; -; Genomic_DNA. DR RefSeq; WP_011917541.1; NC_009437.1. DR AlphaFoldDB; A4XL21; -. DR SMR; A4XL21; -. DR STRING; 351627.Csac_2021; -. DR KEGG; csc:Csac_2021; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_2_9; -. DR OrthoDB; 9807749at2; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000256; 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. FT CHAIN 1..237 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_1000063196" FT ACT_SITE 8 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 130 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" SQ SEQUENCE 237 AA; 26471 MW; BCCB6436F74896EB CRC64; MIVIPAIDII DGKCVRLTQG DYSRVQEYNL DPVQQAKYFE KEGARYLHVV DLDGAKKGSP VNFEVIKRIK ESTSLSVECG GGIRDKKTIN DYLLAGIDYI ILGSVIFKNP EFVEDVLKRF GNERFIASLD FEEGYVKLSG WQEATRISVE EGILHIKKLG FQKLIYTDIK TDGMLKGHNF EAAKYIRSLF DGFLISSGGI SSMNDVLKLK DIGVDGVIIG KALYTGHVKL NEIINLV //