HIS4_CORGL
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 03-AUG-2022, entry version 137.
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; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC 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 / NCIMB
RC 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 / NCIMB
RC 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}.
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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; 58311529; -.
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 OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000000582; 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; -; 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 PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01919; hisA-trpF; 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
