ID HIS4_ECO57 Reviewed; 245 AA. AC Q9S5G4; Q8X8S9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=Z3186, ECs2825; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=O157:H- / 184 / EHEC; RX PubMed=10222209; DOI=10.1006/mpat.1998.0253; RA Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.; RT "Analysis of the genes responsible for the O-antigen synthesis in RT enterohaemorrhagic Escherichia coli O157."; RL Microb. Pathog. 26:235-247(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG57083.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB36248.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AB008676; BAA77741.1; -; Genomic_DNA. DR EMBL; AE005174; AAG57083.1; ALT_INIT; Genomic_DNA. DR EMBL; BA000007; BAB36248.1; ALT_INIT; Genomic_DNA. DR PIR; A98982; A98982. DR PIR; G85827; G85827. DR RefSeq; NP_310852.2; NC_002695.1. DR RefSeq; WP_000586451.1; NZ_VOAI01000013.1. DR AlphaFoldDB; Q9S5G4; -. DR SMR; Q9S5G4; -. DR STRING; 155864.Z3186; -. DR GeneID; 912886; -. DR KEGG; ece:Z3186; -. DR KEGG; ecs:ECs_2825; -. DR PATRIC; fig|386585.9.peg.2960; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_2_6; -. DR OMA; EWLHLVD; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; 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..245 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000142006" FT ACT_SITE 7 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 129 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 245 AA; 26031 MW; 2CF26D4B4C032ADB CRC64; MIIPALDLID GTVVRLHQGD YGKQRDYGND PLPRLQDYAA QGAEVLHLVD LTGAKDPAKR QIPLIKTLVA GVNVPVQVGG GVRSEEDVAA LLEAGVARVV VGSTAVKSPE MVKGWFERFG ADALVLALDV RIDEQGNKQV AVSGWQENSG VSLEQLVETY LPVGLKHVLC TDISRDGTLA GSNVSLYEEV CARYPQVAFQ SSGGIGDIND VAALRGTGVR GVIVGRALLE GKFTVKEAIS CWQNA //