HIS1_SULDN
ID HIS1_SULDN Reviewed; 209 AA.
AC Q30S64;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; OrderedLocusNames=Suden_0889;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01018}.
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DR EMBL; CP000153; ABB44167.1; -; Genomic_DNA.
DR RefSeq; WP_011372519.1; NC_007575.1.
DR AlphaFoldDB; Q30S64; -.
DR SMR; Q30S64; -.
DR STRING; 326298.Suden_0889; -.
DR EnsemblBacteria; ABB44167; ABB44167; Suden_0889.
DR KEGG; tdn:Suden_0889; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_7; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002714; 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 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 PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..209
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000229339"
SQ SEQUENCE 209 AA; 23463 MW; 7687AFA563F0A44B CRC64;
MLTVALPKGR IAQETLEIFE TLFGDGFAFD DRKLILETPK FRFLLVRNQD VATYVFHQAA
DIGVVGLDTL EEQGLDVIRL LDLKRGICKV AIGMKKGEKF DLNKPEIKVA SKMVNITKRY
FEERAVSVDI IKLYGSIELA PLIGLADMIV DVVETGSTMK QNGLEVVEDI MTSSTYLIAN
KNSYIAKKDE VLDIYEKIKS VIDAEQKIK
