ID HIS4_LEUMM Reviewed; 238 AA. AC Q03VX9; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 92. 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=LEUM_1551; OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Leuconostoc. OX NCBI_TaxID=203120; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO RC 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000414; ABJ62643.1; -; Genomic_DNA. DR RefSeq; WP_011680216.1; NC_008531.1. DR AlphaFoldDB; Q03VX9; -. DR SMR; Q03VX9; -. DR EnsemblBacteria; ABJ62643; ABJ62643; LEUM_1551. DR GeneID; 61175975; -. DR KEGG; lme:LEUM_1551; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_2_9; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000362; 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..238 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000290488" FT ACT_SITE 7 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 129 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" SQ SEQUENCE 238 AA; 25713 MW; 3919D844B1F3B095 CRC64; MIFPAIDLLN GQSVRLYQGD YEKETTINPD PLKQAKQIES AGLKHLHLVD LDGAKEGKPV NLNVIQSLRE QTNLFIELGG GIRTLEQVNQ YLNIGINRVI IGSAALTHPE LVRTAVAKYG SDKIVVGVDG RDEKVATQGW LENSDTSFDD IVEAMLSVGV SNFVVTDIAR DGTLSGPNIE LLSRLQNKFP KSNIIASGGI ANIKNVTDLQ ASGIHDIIVG RALYDGDVTL AQLKEVDG //