ID E0URR0_SULAO Unreviewed; 207 AA.
AC E0URR0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946, 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 OrderedLocusNames=Saut_0955 {ECO:0000313|EMBL:ADN09004.1};
OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS OK10).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN09004.1, ECO:0000313|Proteomes:UP000007803};
RN [1] {ECO:0000313|EMBL:ADN09004.1, ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX PubMed=21304749;
RA Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10).";
RL Stand. Genomic Sci. 3:194-202(2010).
RN [2] {ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX DOI=10.4056/sigs.1173118;
RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10T).";
RL Stand. Genomic Sci. 3:194-202(2010).
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|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}.
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DR EMBL; CP002205; ADN09004.1; -; Genomic_DNA.
DR RefSeq; WP_013326760.1; NC_014506.1.
DR AlphaFoldDB; E0URR0; -.
DR STRING; 563040.Saut_0955; -.
DR KEGG; sua:Saut_0955; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_7; -.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000007803; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000007803};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01018}.
FT DOMAIN 47..199
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 207 AA; 23361 MW; 51E6512C3A4E20A5 CRC64;
MLTVALPKGR IAKETLEIFE TIFGEGFKFD DRKLILETPK FRFLLVRNQD VATYVYHQAA
DIGVVGLDTL EEQGLDVVRL LDLRRGVCKV AIGMRKGEKL DLTKPELKVA SKMVNITKRY
FEERAVSVEI IKLYGSIELA PLIGLADMIV DIVETGTTMK QNGLEVVQDI MTSSTYLIAN
KNSYISKKDE VLDIYEKINE VIKAEND
//
