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Database: UniProt
Entry: G4CQL0_9NEIS
LinkDB: G4CQL0_9NEIS
Original site: G4CQL0_9NEIS 
ID   G4CQL0_9NEIS            Unreviewed;       222 AA.
AC   G4CQL0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_01018};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018,
GN   ECO:0000313|EMBL:EGZ46271.1};
GN   ORFNames=HMPREF9370_1370 {ECO:0000313|EMBL:EGZ46271.1};
OS   Neisseria wadsworthii 9715.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ46271.1, ECO:0000313|Proteomes:UP000005336};
RN   [1] {ECO:0000313|EMBL:EGZ46271.1, ECO:0000313|Proteomes:UP000005336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9715 {ECO:0000313|EMBL:EGZ46271.1,
RC   ECO:0000313|Proteomes:UP000005336};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00024861, ECO:0000256|HAMAP-Rule:MF_01018}.
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         Evidence={ECO:0000256|ARBA:ARBA00000915, ECO:0000256|HAMAP-
CC         Rule:MF_01018};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000256|ARBA:ARBA00011496, ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC       HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000256|ARBA:ARBA00009489, ECO:0000256|HAMAP-
CC       Rule:MF_01018}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGZ46271.1}.
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DR   EMBL; AGAZ01000050; EGZ46271.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4CQL0; -.
DR   STRING; 1030841.HMPREF9370_1370; -.
DR   PATRIC; fig|1030841.3.peg.1352; -.
DR   HOGENOM; CLU_038115_2_0_4; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000005336; Unassembled WGS sequence.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13595; PBP2_HisGs; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   HAMAP; MF_01018; HisG_Short; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR   NCBIfam; TIGR00070; hisG; 1.
DR   PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR   Pfam; PF01634; HisG; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01018};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01018}.
FT   DOMAIN          59..214
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
SQ   SEQUENCE   222 AA;  23720 MW;  70ADB2462105B428 CRC64;
     MKDIMQDNSL TIALSKGRIF EETLPLLAAA GIIPAEAPEK SRKLIIETNH SEIRLVIVRA
     SDVPTYVQYG AADFGIAGKD VLIEHGGEGL YQPLDLQIAK CRMMVAVPKG FDYAAASKPG
     CRLRVATKYP DIAAEHFAAK GVHVDIIKLY GSMELAPLVG LSDAIVDLVS TGGTLKANNL
     EAVEHIVDIS SRLVVNKAAL KTKYALIEPI IEAFAGVVAN GK
//
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