HIS1_THEMA
ID HIS1_THEMA Reviewed; 208 AA.
AC Q9X0D2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=TM_1042;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD36119.1; -; Genomic_DNA.
DR PIR; A72305; A72305.
DR RefSeq; NP_228848.1; NC_000853.1.
DR RefSeq; WP_004080478.1; NZ_CP011107.1.
DR PDB; 1O63; X-ray; 2.00 A; A/B=2-208.
DR PDB; 1O64; X-ray; 2.10 A; A/B=2-208.
DR PDB; 1USY; X-ray; 2.52 A; E/F/G/H=1-208.
DR PDBsum; 1O63; -.
DR PDBsum; 1O64; -.
DR PDBsum; 1USY; -.
DR AlphaFoldDB; Q9X0D2; -.
DR SMR; Q9X0D2; -.
DR STRING; 243274.THEMA_09150; -.
DR EnsemblBacteria; AAD36119; AAD36119; TM_1042.
DR KEGG; tma:TM1042; -.
DR eggNOG; COG0040; Bacteria.
DR InParanoid; Q9X0D2; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; Q9X0D2; -.
DR Proteomes; UP000008183; 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; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151944"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 79..93
FT /evidence="ECO:0007829|PDB:1O63"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1USY"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:1O63"
FT STRAND 160..175
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:1O63"
FT HELIX 184..203
FT /evidence="ECO:0007829|PDB:1O63"
SQ SEQUENCE 208 AA; 23511 MW; A3629EF262F48A80 CRC64;
MLKLAIPKGR LEEKVMTYLK KTGVIFERES SILREGKDIV CFMVRPFDVP TYLVHGVADI
GFCGTDVLLE KETSLIQPFF IPTNISRMVL AGPKGRGIPE GEKRIATKFP NVTQRYCESK
GWHCRIIPLK GSVELAPIAG LSDLIVDITE TGRTLKENNL EILDEIFVIR THVVVNPVSY
RTKREEVVSF LEKLQEVIEH DSNEQSRG
