(data stored in SCRATCH zone)

SWISSPROT: C6B2J6_RHILS

ID   C6B2J6_RHILS            Unreviewed;       231 AA.
AC   C6B2J6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|SAAS:SAAS00046302};
DE            EC=2.4.2.17 {ECO:0000256|SAAS:SAAS00046302};
GN   OrderedLocusNames=Rleg_0511 {ECO:0000313|EMBL:ACS54816.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54816.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54816.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54816.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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|SAAS:SAAS00046314}.
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|SAAS:SAAS01121154};
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|SAAS:SAAS00046315}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00046328}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       {ECO:0000256|SAAS:SAAS00586233}.
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DR   EMBL; CP001622; ACS54816.1; -; Genomic_DNA.
DR   RefSeq; WP_012756202.1; NC_012850.1.
DR   EnsemblBacteria; ACS54816; ACS54816; Rleg_0511.
DR   KEGG; rlg:Rleg_0511; -.
DR   HOGENOM; HOG000223249; -.
DR   KO; K00765; -.
DR   OMA; IFNLDNC; -.
DR   OrthoDB; 1419568at2; -.
DR   BioCyc; RLEG395491:GHX2-512-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002256; 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-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
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;
DR   PRODOM; C6B2J6.
DR   SWISS-2DPAGE; C6B2J6.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00046310};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00046309};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00046320};
KW   Glycosyltransferase {ECO:0000256|SAAS:SAAS00046307,
KW   ECO:0000313|EMBL:ACS54816.1};
KW   Histidine biosynthesis {ECO:0000256|SAAS:SAAS00046316};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00046318};
KW   Transferase {ECO:0000256|SAAS:SAAS00046311,
KW   ECO:0000313|EMBL:ACS54816.1}.
FT   DOMAIN       54    227       HisG. {ECO:0000259|Pfam:PF01634}.
SQ   SEQUENCE   231 AA;  25059 MW;  CF7A6A5EB96A695A CRC64;
     MTITIALPSK GRMKEDASAI FERAGMTISA VGNDRSYRGR VEGWDDVEIA FLSASEISRE
     IGNGTVDFGV TGEDLMREGF AEVDKRVEFC ARLGFGHADV VVAVPEIWLD VDTMADLVDV
     AADFRARHSR RLAIATKYWR LTQQFFSSQH GIQLYRIVES LGATEGAPAS GSADIIVDIT
     STGSTLRANH LKVLQDGVIL HSQACLVRAR KESHAGEPAV QAIIDAVRAA L
//

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