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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//