ID C8X0P9_DESRD Unreviewed; 797 AA.
AC C8X0P9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:ACV67996.1};
GN OrderedLocusNames=Dret_0704 {ECO:0000313|EMBL:ACV67996.1};
OS Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 /
OS HR100).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfohalobiaceae; Desulfohalobium.
OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV67996.1, ECO:0000313|Proteomes:UP000001052};
RN [1] {ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Desulfohalobium retbaense DSM 5692.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV67996.1, ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV67996.1,
RC ECO:0000313|Proteomes:UP000001052};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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DR EMBL; CP001734; ACV67996.1; -; Genomic_DNA.
DR RefSeq; WP_015751154.1; NC_013223.1.
DR AlphaFoldDB; C8X0P9; -.
DR STRING; 485915.Dret_0704; -.
DR KEGG; drt:Dret_0704; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_7; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000001052; 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; 1.
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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:ACV67996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001052}.
FT DOMAIN 53..262
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 716..785
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 797 AA; 89101 MW; 109A08DBBE7ACB2E CRC64;
MTAHWLPLDH PASTRADDVG HKCANLAQAR EKGFAIPPAV VIPVQAHRYY HHEKKWPDGL
RASIIQAAQH LGLDAGVAVR SSGTREDLGE HSFAGQYATL LDVRDPQALL GAVEACWSSQ
ESDQVRAYQD QHEGSGQAGW VAVLIQKMVP ARHAGVAFSR NPLFPARAET IVEAVDGLGE
GLVNGQRSPV RATLRDKEPV RVEEASSNTP SVALADETWR RIGAMAMTLE QHFGHPQDIE
WAEDHEGTLW LLQSRPISTI RPEDMRIPAG LWTRKIANDL WSDRLTPFLA REMERNASRF
DLSRAAGWLG IPVARPSVRV INGFLYVNAE RITAILQGIP KNFRLSNLSS LVPPSRRVDL
GPTKWSRVVS SSLRALLFFA GNPWANPLSS GLVNRIHRHL MGGKLRRQGR RSVQTPGQSL
AAIDTDLALL ARNQQRNQWP YAYATGLTWT LQWVLEEKLG LNQEVFLTLL NKRGDNVTLR
IERTLRTLAE RIARNPALRH RFQTEPIERL RFNLPQWLQI ELANFMNRYG CRSPHRTLTV
PRWEEDPGQV LAFLRSLSAE PRSGTNAPRA SIDAWRQIPL FWRPFVWILL RATRSFLDLR
EELRFVLDKN LCLLRRHLLR LGKQTGLGEH IVFLTREELQ TLVHSPEERD RLIGLAEERI
QRHRQSEYAP VYYSDGRAEE EFMIQEGSLQ GIGTSAGQTS GTAQIVQDPS EVRLRGEVIV
VAAHTDPGWT PLLSLVKGLI VEEGGLLSHC AIVARELGIP AVVGVHRATT RIPDGAQVSL
NGATGHIAIA TDPASPN
//
