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Database: UniProt
Entry: C1BDT0_RHOOB
LinkDB: C1BDT0_RHOOB
Original site: C1BDT0_RHOOB 
ID   C1BDT0_RHOOB            Unreviewed;       542 AA.
AC   C1BDT0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Putative pyruvate, phosphate dikinase {ECO:0000313|EMBL:BAH47133.1};
DE            EC=2.7.9.1 {ECO:0000313|EMBL:BAH47133.1};
GN   OrderedLocusNames=ROP_pROB02-01200 {ECO:0000313|EMBL:BAH47133.1};
OS   Rhodococcus opacus (strain B4).
OG   Plasmid pROB02 {ECO:0000313|EMBL:BAH47133.1,
OG   ECO:0000313|Proteomes:UP000002212}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH47133.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH47133.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH47133.1,
RC   ECO:0000313|Proteomes:UP000002212};
RC   PLASMID=pROB02 {ECO:0000313|EMBL:BAH47133.1};
RX   PubMed=16233805; DOI=10.1263/jbb.99.378;
RA   Na K.S., Kuroda A., Takiguchi N., Ikeda T., Ohtake H., Kato J.;
RT   "Isolation and characterization of benzene-tolerant Rhodococcus opacus
RT   strains.";
RL   J. Biosci. Bioeng. 99:378-382(2005).
RN   [2] {ECO:0000313|EMBL:BAH47133.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH47133.1,
RC   ECO:0000313|Proteomes:UP000002212};
RC   PLASMID=pROB02 {ECO:0000313|EMBL:BAH47133.1,
RC   ECO:0000313|Proteomes:UP000002212};
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 erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP011117; BAH47133.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1BDT0; -.
DR   KEGG; rop:ROP_pROB02-01200; -.
DR   PATRIC; fig|632772.20.peg.8500; -.
DR   HOGENOM; CLU_015345_2_0_11; -.
DR   Proteomes; UP000002212; Plasmid pROB02.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.80.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 3.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAH47133.1};
KW   Plasmid {ECO:0000313|EMBL:BAH47133.1};
KW   Pyruvate {ECO:0000313|EMBL:BAH47133.1};
KW   Transferase {ECO:0000313|EMBL:BAH47133.1}.
FT   DOMAIN          27..65
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          66..282
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          293..344
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          418..499
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   542 AA;  58539 MW;  C8D3A9083C2E4414 CRC64;
     MGDAAPLTAA IYPFDHPHRA RPRALTDLLG GKGAGLAEMI STLGINVPPG FTISVPLCQR
     YRREGWPEGL DEAITLHTSR LGDRMGRRFG DHNDPLLVAV RSGAPVSMPG MLDTVLNLGL
     NEYTVEGLAK VSGDEKFAWD SYRRFLHMYA TTVMGVHCDE LYVGHSGDTT ESLREHVVLL
     RERIRQVAGR DVPAEPTVQL REAVEAVFRS WDSQRARTYR AKEGIDESMG TAVNVQAMVF
     GNRGLNSGTG VVFTRDPSTG EAVLYGDYLP MAQGEDVVAG TAHTLPIADL EQLHPAIYTE
     LQETLRRLEV HYRDVCDVEF TIENGRLWLL QTRAGKRSAV AAVRIAVDLV NDPDIRLTPT
     EAVSRVPAAV RQRARDEALA HVGADDAAHD LVTTGLGASP GRAVGRVVLT SDEAADADDD
     VILVRPETKP EDVAGMAASV GLLTTKGGLV SHAAVVARGW NIPAVVGAQD LTCSANGIHA
     PSGLLIRVGD VITIDGTTGQ VWRGAVTTPT DEIVIRAIEH ELPQLPALEE WARQYAHEGE
     EQ
//
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