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Database: UniProt
Entry: B9LU14
LinkDB: B9LU14
Original site: B9LU14 
ID   HIS1_HALLT              Reviewed;         296 AA.
AC   B9LU14;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   26-NOV-2014, entry version 41.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_00079};
GN   OrderedLocusNames=Hlac_2637;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 /
OS   ACAM 34).
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Anderson I., DasSarma S., Cavicchioli R., Richardson P.;
RT   "Complete sequence of chromosome1 of Halorubrum lacusprofundi ATCC
RT   49239.";
RL   Submitted (JAN-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:0000255|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:0000255|HAMAP-Rule:MF_00079}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00079};
CC   -!- ENZYME REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Long subfamily. {ECO:0000255|HAMAP-Rule:MF_00079}.
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DR   EMBL; CP001365; ACM58208.1; -; Genomic_DNA.
DR   RefSeq; YP_002567278.1; NC_012029.1.
DR   ProteinModelPortal; B9LU14; -.
DR   STRING; 416348.Hlac_2637; -.
DR   EnsemblBacteria; ACM58208; ACM58208; Hlac_2637.
DR   GeneID; 7400842; -.
DR   KEGG; hla:Hlac_2637; -.
DR   eggNOG; COG0040; -.
DR   HOGENOM; HOG000223247; -.
DR   KO; K00765; -.
DR   OMA; TRMQGVI; -.
DR   BioCyc; HLAC416348:GIWW-2692-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    296       ATP phosphoribosyltransferase.
FT                                /FTId=PRO_1000118254.
SQ   SEQUENCE   296 AA;  31201 MW;  AB5FB5682994BDBA CRC64;
     MRIAVPNKGR LHDPTLSLLE RAGLHTEETA DRQLYADTVD PDVSILFARA ADIPEYVRDG
     AADVGITGLD QAAESGGVAD SASAAGDDDL VDLLDLGYGS CKLVLAAPED GDISVVADLA
     GGTVATEFPN ITRDYLDRVD VDADVVTVTG ATELTPHVDM ADAIVDITST GTTLKVNRLA
     VIDDVLDSSV RLFARPDMVD DAKVKQVLTA FESVLAADGR RYLMMNAPKE RLDEVKDVIP
     GLGGPTVMDV EADENGNGMV AVHAVVEERD VFATISELKS VGATGILVTK IERLVG
//
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