(data stored in ACNUC7421 zone)

SWISSPROT: HIS1_SINFN

ID   HIS1_SINFN              Reviewed;         231 AA.
AC   C3MGT4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=NGR_c04030;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced
CC       by HisZ.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Short subfamily. {ECO:0000305}.
DR   EMBL; CP001389; ACP24199.1; -; Genomic_DNA.
DR   RefSeq; WP_012706984.1; NC_012587.1.
DR   RefSeq; YP_002824952.1; NC_012587.1.
DR   STRING; 394.NGR_c04030; -.
DR   EnsemblBacteria; ACP24199; ACP24199; NGR_c04030.
DR   GeneID; 7791629; -.
DR   KEGG; rhi:NGR_c04030; -.
DR   PATRIC; fig|394.7.peg.3209; -.
DR   eggNOG; ENOG4105E21; Bacteria.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223249; -.
DR   KO; K00765; -.
DR   OMA; IFNLDNC; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001054; 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; C3MGT4.
DR   SWISS-2DPAGE; C3MGT4.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    231       ATP phosphoribosyltransferase.
FT                                /FTId=PRO_1000213276.
SQ   SEQUENCE   231 AA;  24896 MW;  7B6FAB16521EBBAE CRC64;
     MTITIALPSK GRMKDDASAI FERAGMKIVA VGNDRSYRGR VEGWDDVEVA FLSASEISRE
     VGSGAVDFGV TGEDLVREGI ADVDARVEFA ARLGFGHADV VVAVPEVWYD VDTMADLGDV
     AADFRARHGR RLAIATKYWR LTQQFFSGSH GIQLYRIVES LGATEGAPAS GSADIIVDIT
     STGSTLKANH LKILSDGVIL RSEACLVRAR KPAHDGYPMI DRIISSVRSV L
//

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