ID HIS4_ZYMMO Reviewed; 250 AA. AC Q5NMD5; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 104. 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=ZMO1501; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Zymomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., RA Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). 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; AE008692; AAV90125.2; -; Genomic_DNA. DR RefSeq; WP_011241274.1; NZ_CP035711.1. DR AlphaFoldDB; Q5NMD5; -. DR SMR; Q5NMD5; -. DR STRING; 264203.ZMO1501; -. DR KEGG; zmo:ZMO1501; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_1_5; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000001173; 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..250 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000229098" FT ACT_SITE 12 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" FT ACT_SITE 133 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014" SQ SEQUENCE 250 AA; 26147 MW; 1165286F527EF6A3 CRC64; MTDSLIIFPA IDLKEGHVVR LSEGDMDRAT IYDDDPAARA RQFYEAGARY LHVVDLDGAF AGHAMNAAAV DAIVKAFPGT IELGGGIRDM NAIDGWLSRG ISRVVIGTAA FENPDLVKEA AQKYPGQIVV AVDARDGMVT TKGWAEQSEI SVTDMAERFA DAGVVALLYT DVGRDGLKKG CNSEATLALA AATDIPVIAS GGVKDIGDIE LLARHTKDGI EGVICGRAIY DGSLDLKAAL AIARQGGASA //