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Database: UniProt/TrEMBL
Entry: D0LDS2_GORB4
LinkDB: D0LDS2_GORB4
Original site: D0LDS2_GORB4 
ID   D0LDS2_GORB4            Unreviewed;       281 AA.
AC   D0LDS2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   26-NOV-2014, entry version 36.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079};
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};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079};
GN   OrderedLocusNames=Gbro_2454 {ECO:0000313|EMBL:ACY21695.1};
OS   Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC
OS   10667) (Rhodococcus bronchialis).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY21695.1, ECO:0000313|Proteomes:UP000001219};
RN   [1] {ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667
RC   {ECO:0000313|Proteomes:UP000001219};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Goeker M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
CC       = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00031006}.
CC   -!- COFACTOR:
CC       Note=Magnesium. {ECO:0000256|HAMAP-Rule:MF_00079};
CC   -!- ENZYME 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:SAAS00031008}.
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; CP001802; ACY21695.1; -; Genomic_DNA.
DR   RefSeq; WP_012834250.1; NC_013441.1.
DR   RefSeq; YP_003273588.1; NC_013441.1.
DR   STRING; 526226.Gbro_2454; -.
DR   EnsemblBacteria; ACY21695; ACY21695; Gbro_2454.
DR   GeneID; 8551818; -.
DR   KEGG; gbr:Gbro_2454; -.
DR   PATRIC; 32184519; VBIGorBro114338_2510.
DR   eggNOG; COG0040; -.
DR   HOGENOM; HOG000223250; -.
DR   KO; K00765; -.
DR   OMA; YVMLDYD; -.
DR   OrthoDB; EOG66MQT3; -.
DR   BioCyc; GBRO526226:GHJF-2487-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
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-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
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;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00031010};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001219};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00021142};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00031015};
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:UP000001219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00031009}.
SQ   SEQUENCE   281 AA;  30093 MW;  AC4FB0D5B55808F4 CRC64;
     MLRVAVPNKG ALSESASAIL AEAGYRKRSD AKDLTVLDNT NDVEFFFLRP KDIAIYVGAG
     TLDLGITGRD LAGDSGASVD EELSMGFGSS TFRYAAPAGS PWCVADLAGK RIATSYPNLV
     RADLERRGIE AEIIRLDGAV EISIQLGVAD AIADVVGSGR TLRQHGLVAF GDSLCDSEAV
     LISRTGTANE KAARQFIARV QGVVFGQQYV MIDYDCPRSL LDQATELTPG LESPTVAPMA
     DPDWVAVRAM VPRRDHQNLM DQLSDLGARA ILATDIRSCR F
//
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