ID HIS4_CORGL Reviewed; 246 AA. AC O68602; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 26-JUL-2002, sequence version 2. DT 27-MAR-2024, entry version 145. 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=Cgl2096, cg2299; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613; RX PubMed=9647764; DOI=10.1006/bbrc.1998.8850; RA Jung S.-I., Han M.-S., Kwon J.-H., Cheon C.-I., Min K.-H., Lee M.-S.; RT "Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum: RT organization and sequencing analysis of the hisA, impA, and hisF gene RT cluster."; RL Biochem. Biophys. Res. Commun. 247:741-745(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC -!- CAUTION: Ala-129 is present instead of the conserved Asp which is CC expected to be an active site residue. {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; AF051846; AAC05575.1; -; Genomic_DNA. DR EMBL; BA000036; BAB99489.1; -; Genomic_DNA. DR EMBL; BX927154; CAF20432.1; -; Genomic_DNA. DR PIR; JE0213; JE0213. DR RefSeq; NP_601295.1; NC_003450.3. DR RefSeq; WP_003856418.1; NC_006958.1. DR AlphaFoldDB; O68602; -. DR SMR; O68602; -. DR STRING; 196627.cg2299; -. DR GeneID; 69623420; -. DR KEGG; cgb:cg2299; -. DR KEGG; cgl:Cgl2096; -. DR PATRIC; fig|196627.13.peg.2032; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_1_11; -. DR OrthoDB; 9807749at2; -. DR BioCyc; CORYNE:G18NG-11688-MONOMER; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; 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:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro. 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; IPR010188; HisA/PriA_Actinobacteria. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR01919; hisA-trpF; 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..246 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000142001" FT ACT_SITE 10 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT CONFLICT 82 FT /note="G -> S (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" FT CONFLICT 90..92 FT /note="ERA -> DTQ (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="A -> L (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" FT CONFLICT 119..127 FT /note="RYGEKIAVD -> AMARRLLS (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="R -> C (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" FT CONFLICT 195..198 FT /note="PIVA -> TYLT (in Ref. 1; AAC05575)" FT /evidence="ECO:0000305" SQ SEQUENCE 246 AA; 26609 MW; 6A35CF9153C32B1E CRC64; MTFTILPAVD VVNGQAVRLD QGEAGTEKSY GTPLESALKW QEQGAKWLHF VDLDAAFNRG SNHEMMAEIV GKLDVDVELT GGIRDDESLE RALATGARRV NIGTAALEKP EWIASAIQRY GEKIAVDIAV RLEDGEWRTR GNGWVSDGGD LWEVLERLDS QGCARFVVTD VSKDGTLSGP NVELLREVAA ATDAPIVASG GISVLEDVLE LAKYQDEGID SVIIGKALYE HKFTLEEALA AVEKLG //