ID V9XN05_9NOCA Unreviewed; 840 AA.
AC V9XN05;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:AHD23439.1};
GN ORFNames=Y013_24060 {ECO:0000313|EMBL:AHD23439.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD23439.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD23439.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD23439.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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DR EMBL; CP006996; AHD23439.1; -; Genomic_DNA.
DR RefSeq; WP_024103627.1; NC_023150.1.
DR AlphaFoldDB; V9XN05; -.
DR GeneID; 29940264; -.
DR KEGG; rpy:Y013_24060; -.
DR PATRIC; fig|1435356.3.peg.4849; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_11; -.
DR Proteomes; UP000018781; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 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 PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 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.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:AHD23439.1}.
FT DOMAIN 16..232
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 235..288
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 763..834
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 840 AA; 92059 MW; 9554FA28A410B420 CRC64;
MGYIQNFREI DRTAVSIVGG KGASLGELWR LDDVDVPDGF CVTTDAYRTV LSELPCVDDL
LERLAKAEPD DIAALSTQIR TAIEECTIPG DIAEEIAARV RELGEDVPVA VRSSATAEDL
PTVSFAGQQD SYLDIRGVED VLRHVSRCWA SLFTERAVAY RVNNGFDHRK VYMAVVVQRM
VFPQASGVLF TADPVTSDRT VSRVDAVAGL GDDLVSGLVN ADAYAVRADE VVDRTQRQET
PVLSDTHLVE LVGLGRRLEA HFGRPQDIEW CLADGVFHIV QSRPITTLFP VPEAGDDDNH
VYLSVGHQQM MTDPLKPLGI SVWQLTSRAP MRHAGGRLFV DVTPMLASPT QGPGIVDMIG
RSDPLFGDAL RTVLDRGFVP TRPDDPAAAP VGLPPVPDEI DPAVVPELVA RNEAAIAESA
RRIENETGSA LLDFIRADIR ELQDSLFGKE VGEVLAAGMQ AAERLNEVGQ KWLGEKNVAD
VVSRSVPYNV TSEMGLALLD VADAARPYPD VVAFLRQVDE EGFDDARFLD ELGTRDGGPQ
VRAALEDFLD KYGRRCVGEI DITRPRWGER PTMLVPMIVS NLDNFETGAA TQCFDNGRRQ
AEEKKGELLE RVRGLPDGEQ KEREIERLVD RVRAFAGYRE YPKYGMIGRY FVYKQALLRE
AERLVRAGVI DDEEDIFFLR FDELEDVVRA PQPVGDLVAE RKREFASFAT LTPPRVLLST
GETLTGAYSR DGLPDGALPG IAVSTGVVEG RARVVTDMDR ADLEPGDILV TAFTDPSWTP
AFVTVSALVT EVGGVMTHGA VIAREYGLPA VVGVEDATRL IRDGQRIRVH GTEGYVEILT
//
