(data stored in ACNUC7421 zone)

SWISSPROT: HIS2_RHOOB

ID   HIS2_RHOOB              Reviewed;          93 AA.
AC   C1ASQ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020};
DE            Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020};
DE            EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020};
GN   Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020};
GN   OrderedLocusNames=ROP_05930;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1-
CC       (5-phospho-beta-D-ribosyl)-AMP + diphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01020}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}.
CC   -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_01020}.
DR   EMBL; AP011115; BAH48840.1; -; Genomic_DNA.
DR   ProteinModelPortal; C1ASQ8; -.
DR   SMR; C1ASQ8; -.
DR   STRING; 632772.ROP_05930; -.
DR   EnsemblBacteria; BAH48840; BAH48840; ROP_05930.
DR   KEGG; rop:ROP_05930; -.
DR   PATRIC; fig|632772.20.peg.651; -.
DR   eggNOG; ENOG4105M0N; Bacteria.
DR   eggNOG; COG0140; LUCA.
DR   HOGENOM; HOG000220966; -.
DR   KO; K01523; -.
DR   OMA; VWMAAEY; -.
DR   OrthoDB; POG091H09PQ; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01020; HisE; 1.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   Pfam; PF01503; PRA-PH; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASQ8.
DR   SWISS-2DPAGE; C1ASQ8.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Nucleotide-binding.
FT   CHAIN         1     93       Phosphoribosyl-ATP pyrophosphatase.
FT                                /FTId=PRO_1000149059.
SQ   SEQUENCE   93 AA;  10356 MW;  2E3A79D382B99FA3 CRC64;
     MKEWVLVKTF ESLFAELTER AATRPEGSGT VAALDAGVHS QGKKILEEAG EVWIAAEHES
     DEALAEEISQ LLYWTQVLMV GKGLKLEDVY RHL
//

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