ID   HIS1_CORGL              Reviewed;         281 AA.
AC   Q9Z472;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=Cgl1504, cg1698;
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=11006846; DOI=10.1139/w00-065;
RA   Kwon J.H., Chun J.Y., Lee H.S., Cheon C.I., Song E.S., Min K.H., Lee M.-S.;
RT   "Cloning of the histidine biosynthetic genes from Corynebacterium
RT   glutamicum: organization and analysis of the hisG and hisE genes.";
RL   Can. J. Microbiol. 46:848-855(2000).
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   -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC       diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC       role in the pathway because the rate of histidine biosynthesis seems to
CC       be controlled primarily by regulation of HisG enzymatic activity (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC         alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:73183; EC=2.4.2.17;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF050166; AAD02497.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98897.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21512.1; -; Genomic_DNA.
DR   RefSeq; NP_600720.1; NC_003450.3.
DR   RefSeq; WP_003856149.1; NC_006958.1.
DR   AlphaFoldDB; Q9Z472; -.
DR   SMR; Q9Z472; -.
DR   STRING; 196627.cg1698; -.
DR   World-2DPAGE; 0001:Q9Z472; -.
DR   GeneID; 58309304; -.
DR   KEGG; cgb:cg1698; -.
DR   KEGG; cgl:Cgl1504; -.
DR   PATRIC; fig|196627.13.peg.1471; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_1_11; -.
DR   OMA; YVMMDYD; -.
DR   BRENDA; 2.4.2.17; 960.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.120; -; 1.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; SSF54913; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
DR   TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..281
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151846"
FT   CONFLICT        10
FT                   /note="G -> A (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="G -> A (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="Missing (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="D -> Y (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="A -> R (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..165
FT                   /note="RQQ -> LT (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="L -> C (in Ref. 1; AAD02497)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  30229 MW;  62DF8724CBE9B78C CRC64;
     MLKIAVPNKG SLSERAMEIL AEAGYAGRGD SKSLNVFDEA NNVEFFFLRP KDIAIYVAGG
     QLDLGITGRD LARDSQADVH EVLSLGFGSS TFRYAAPADE EWSIEKLDGK RIATSYPNLV
     RDDLAARGLS AEVLRLDGAV EVSIKLGVAD AIADVVSTGR TLRQQGLAPF GEVLCTSEAV
     IVGRKDEKVT PEQQILLRRI QGILHAQNFL MLDYNVDRDN LDAATAVTPG LSGPTVSPLA
     RDNWVAVRAM VPRRSANAIM DKLAGLGAEA ILASEIRIAR I