(data stored in ACNUC7421 zone)

SWISSPROT: Q47TK2_THEFY

ID   Q47TK2_THEFY            Unreviewed;       284 AA.
AC   Q47TK2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079};
GN   OrderedLocusNames=Tfu_0174 {ECO:0000313|EMBL:AAZ54212.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54212.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC       diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a
CC       crucial role in the pathway because the rate of histidine
CC       biosynthesis seems to be controlled primarily by regulation of
CC       HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + ATP;
CC         Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00079,
CC         ECO:0000256|SAAS:SAAS01121154};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00079};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046315}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Long subfamily. {ECO:0000256|HAMAP-Rule:MF_00079}.
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DR   EMBL; CP000088; AAZ54212.1; -; Genomic_DNA.
DR   RefSeq; WP_011290621.1; NC_007333.1.
DR   STRING; 269800.Tfu_0174; -.
DR   EnsemblBacteria; AAZ54212; AAZ54212; Tfu_0174.
DR   KEGG; tfu:Tfu_0174; -.
DR   eggNOG; ENOG4105E21; Bacteria.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223250; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 1419568at2; -.
DR   BioCyc; TFUS269800:G1G4Q-177-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000434; 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;
DR   PRODOM; Q47TK2.
DR   SWISS-2DPAGE; Q47TK2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046310};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00426273, ECO:0000313|EMBL:AAZ54212.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046316};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:AAZ54212.1}.
FT   DOMAIN       52    205       HisG. {ECO:0000259|Pfam:PF01634}.
FT   DOMAIN      209    279       HisG_C. {ECO:0000259|Pfam:PF08029}.
SQ   SEQUENCE   284 AA;  31206 MW;  70A7F6DA7CDB6558 CRC64;
     MTDLLRIAVP NKGQLSEPAI AMLREAGYRQ RKDSRDLVLL DPDNGAEFFF LRPKDIAVYV
     GEGILHVGIT GRDMLIDSGA PVEEVLALGF GNSTFRFAAR NGSSMTVEDL AGKRIATSYE
     GLLTSYLKKR GIEARVIHLD GAVESSIQLG VADAVADVVS TGTTLRQAGL EPFGEPILES
     EAVVIRRKGE PDDPKVEQLL RRLRGVLVAR DYVMMDYDVH AEHLEEAIAL TPGMEGPTVS
     PLHREGWVAV RAMVPRRDAQ RIMDDLWEIG ARAILVTDIY ACRL
//

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