ID C1B3K1_RHOOB Unreviewed; 487 AA.
AC C1B3K1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Putative pyruvate, phosphate dikinase {ECO:0000313|EMBL:BAH50699.1};
DE EC=2.7.9.1 {ECO:0000313|EMBL:BAH50699.1};
GN OrderedLocusNames=ROP_24520 {ECO:0000313|EMBL:BAH50699.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50699.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH50699.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH50699.1,
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; AP011115; BAH50699.1; -; Genomic_DNA.
DR RefSeq; WP_012689655.1; NC_012522.1.
DR AlphaFoldDB; C1B3K1; -.
DR STRING; 632772.ROP_24520; -.
DR KEGG; rop:ROP_24520; -.
DR PATRIC; fig|632772.20.peg.2564; -.
DR HOGENOM; CLU_015345_2_1_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000002212; Chromosome.
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; 3.30.1490.20; ATP-grasp fold, A domain; 2.
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; IPR018274; PEP_util_AS.
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; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAH50699.1};
KW Pyruvate {ECO:0000313|EMBL:BAH50699.1};
KW Transferase {ECO:0000313|EMBL:BAH50699.1}.
FT DOMAIN 61..238
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 253..304
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 373..441
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 487 AA; 51866 MW; 3EE400522ABB66A9 CRC64;
MTVLRLGQCP DAERELIGGK AFSINSMLTL GLPVPPAFVL GTDECARYYA SDRKLADDVL
TELRRGIESL ESTLGRTFGA AQKPLLVSVR SGAPRSMPGM MDTVLNLGIN DAVEAALRDE
TADSDYAADT HRRFKEQFRK VVGSDPSPEP WEQLEAAVAA VFNSWHSPRA VAYRRHHGIS
DDGGTAVTVQ AMVFGNLDDH SGTGVLFTRD PVTAQSAPFG EWLPKGQGED VVSGRCTPLT
LGHLAESMPE VHKQLMESAD LLERTFRDVQ DIEFTVESGH LWLLQTRSAK RSASAAVHHA
VTFEKEGIVT PEGALSMISP EQLSAFLRPH LAPTARIGAT LLARGEVACP GVVTGLVVGT
ADEAEEMAEQ GIDVILARPT TDPDDVHGIL AAKAIITEIG GATSHAAVVS REFNRACVVG
CGEGSLMSLV GKNVTVDASA GEIFDGVLEV EIPSKDTHPD LRVVTEWLAA SATGCDNPLN
KILAAAH
//
