(data stored in ACNUC7421 zone)

SWISSPROT: HIS1_ANADE

ID   HIS1_ANADE              Reviewed;         221 AA.
AC   Q2IMV6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018};
GN   OrderedLocusNames=Adeh_0363;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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_01018}.
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:0000255|HAMAP-Rule:MF_01018};
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_01018}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
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:0000255|HAMAP-Rule:MF_01018}.
DR   EMBL; CP000251; ABC80139.1; -; Genomic_DNA.
DR   RefSeq; WP_011419422.1; NC_007760.1.
DR   STRING; 290397.Adeh_0363; -.
DR   EnsemblBacteria; ABC80139; ABC80139; Adeh_0363.
DR   KEGG; ade:Adeh_0363; -.
DR   eggNOG; ENOG4105E21; Bacteria.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223248; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   BioCyc; ADEH290397:G1G5W-373-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001935; 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-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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; Q2IMV6.
DR   SWISS-2DPAGE; Q2IMV6.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    221       ATP phosphoribosyltransferase.
FT                                /FTId=PRO_0000319512.
SQ   SEQUENCE   221 AA;  23456 MW;  D6A549F5850C4ECE CRC64;
     MPGTSELITV AVPKGRLLQE SSALFERALG VSPRKLLEGT RKLAADAPEA GLRFISIRAG
     DVASYVEHGA AEVGIVGLDV LREEPRDLYE PLDLGIGRCT VIVARPKGAR PLPRGVAPRV
     ATKYLSLAAR HFAAKGVPAE IIPLHGSIEV APSLGLADTI VDITETGETL RANGLVIEEK
     VLEVSARLVV NRVALKLHPE RLRLLIEALR AAVAAADAEA R
//

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