(data stored in SCRATCH zone)

SWISSPROT: A8LDZ6_FRASN

ID   A8LDZ6_FRASN            Unreviewed;       282 AA.
AC   A8LDZ6;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
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=Franean1_0295 {ECO:0000313|EMBL:ABW09761.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09761.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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}.
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; CP000820; ABW09761.1; -; Genomic_DNA.
DR   STRING; 298653.Franean1_0295; -.
DR   EnsemblBacteria; ABW09761; ABW09761; Franean1_0295.
DR   KEGG; fre:Franean1_0295; -.
DR   eggNOG; ENOG4105E21; Bacteria.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223250; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   BioCyc; FSP298653:G1G9X-293-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001313; 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; A8LDZ6.
DR   SWISS-2DPAGE; A8LDZ6.
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:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00426273, ECO:0000313|EMBL:ABW09761.1};
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:UP000001313};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:ABW09761.1}.
FT   DOMAIN       50    202       HisG. {ECO:0000259|Pfam:PF01634}.
FT   DOMAIN      207    278       HisG_C. {ECO:0000259|Pfam:PF08029}.
SQ   SEQUENCE   282 AA;  30197 MW;  7BA80B80D1DA196F CRC64;
     MMLRIAVPNK GGLAAASSQL LCDAGYLARR ESAELVVADV ENDIEFFFLR PRDIAVYVGT
     GRLDLGITGR DLLVDSNTSA QELVPLGFGQ SAFHYAAPAG TMSDIKELDG LRVATSFPGL
     VRTDLAGRGI SVQIVKLDGA VETAVRLGVA DAVADVVETG RTLRAAGLEL VGESVLRSEA
     IMIAKRGADL SAAHERLLRR VQGVLVARRY VMMDYDVPSS VLEKACEVTP GYESPTISPL
     QREGWVAVRA MVLKADVNRT MDDLWDLGAR GILVSGIQAC RL
//

If you have problems or comments...

PBIL Back to PBIL home page