(data stored in SCRATCH zone)

SWISSPROT: D4YXN2_SPHJU

ID   D4YXN2_SPHJU            Unreviewed;       220 AA.
AC   D4YXN2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00008790};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00046302};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018,
GN   ECO:0000313|EMBL:BAI95114.1};
GN   OrderedLocusNames=SJA_C1-02800 {ECO:0000313|EMBL:BAI95114.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95114.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95114.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(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: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
CC       = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00046298}.
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_01018, ECO:0000256|SAAS:SAAS00046315}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00008816}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01018,
CC       ECO:0000256|SAAS:SAAS00046328}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced
CC       by HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Short subfamily. {ECO:0000256|SAAS:SAAS00586253}.
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DR   EMBL; AP010803; BAI95114.1; -; Genomic_DNA.
DR   RefSeq; WP_013038913.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02800; -.
DR   EnsemblBacteria; BAI95114; BAI95114; SJA_C1-02800.
DR   GeneID; 29271983; -.
DR   KEGG; sjp:SJA_C1-02800; -.
DR   eggNOG; ENOG4105E21; Bacteria.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223248; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; POG091H05D7; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000007753; Chromosome 1.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd13595; PBP2_HisGs; 1.
DR   HAMAP; MF_01018; HisG_Short; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
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; D4YXN2.
DR   SWISS-2DPAGE; D4YXN2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046310};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046309};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046320};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046307, ECO:0000313|EMBL:BAI95114.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046316};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046318};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:BAI95114.1}.
FT   DOMAIN       56    208       HisG. {ECO:0000259|Pfam:PF01634}.
SQ   SEQUENCE   220 AA;  23915 MW;  46B842252A166608 CRC64;
     MTRPLTFAIP KGRILDEALP LLAQAGIEPE AEFHDKKSRA LRFATNRPDV SIIRVRAFDV
     ATFVAHGAAQ IGIVGSDVLE EFDYSEIYAP VDLDMGHCRL SVAEPEGLAD EDEAAMSHVR
     VATKYPYLTR KYYEARGIQA ECVKLNGAME LAPSLGLSRR IVDLVSSGAT LKANGLVETN
     VIMAVSARLI VNRAAYKMRS AELVPLVEAF RRAVGGKDAA
//

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