ID S7UPD4_DESML Unreviewed; 1403 AA.
AC S7UPD4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:EPR35859.1};
GN ORFNames=dsmv_0564 {ECO:0000313|EMBL:EPR35859.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR35859.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR35859.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR35859.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPR35859.1}.
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DR EMBL; ATHJ01000105; EPR35859.1; -; Genomic_DNA.
DR STRING; 897.B2D07_15470; -.
DR PATRIC; fig|1121405.3.peg.3269; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR Proteomes; UP000014977; Unassembled WGS sequence.
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:InterPro.
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 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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EPR35859.1};
KW Pyruvate {ECO:0000313|EMBL:EPR35859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW Transferase {ECO:0000313|EMBL:EPR35859.1}.
FT DOMAIN 960..1262
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 1311..1391
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 1403 AA; 160791 MW; 24DE78D76C5FC94A CRC64;
MIRSQALEVN LASYHVEVEI DPRYTVLQEV MAKYYGLMEG MNTFLKELSH PRRNLQFIVD
EARGYALKYF YLLKTHPEGP RAASLYVDIF LDAIHSTADP EVLRDAIDNL LLFIQKTAKD
AGSDHIERFM PVLDDAFRRI RALDDAAFFL FVTSYYPMEK IGEELILHTK EIALDLKELN
ALLFKYFQFT YAYWLGIEDP MEWFEKQVKQ VTDRDRLMDI FETVSHRQIE ALKVELDGIG
HIDVDAAVDK QLYQLSQLLT LPGYSHFTDV YREIPQKLLH SGRDQSQGNR RKVIFLFHIM
NIAGLALIHE EALRDINRTL GWLIGNEKYT YIEKLIKDTF SILKARTREF PQTALSCILN
MGKGLYKTDE LDLVKSFINH VSELGFQAPM IRGVGNDWQI RVNPAHIQNI RTWLELIELN
PKWSTRLLSD LIIHLSLTGV FIKDTDLFPR DITGLLNSDI GPVYNLVKQL ARLFPVYFND
IGAEGALRDI STNIDEIAHR KDPLIHFLRK QAHVESSNRV VSFIEATLRF WLTLDKRHIE
PFVPPSIFEQ IDAHGRHVRD LHKILTHLRE KGLHLPEDLL SRGKTDLDRL LADLPPVPEH
ELERMTLAIH FYQLLHRKYS LILAPEACED LNNYLSQLRS DGFPGVDRLN TMLREDDISG
KLHGLLGYLE ELKALILSKE TYEIREDIYK KRHITVDIPS MYGSYHEMKF NALGLTFRVE
SVVNVCFEEV VDQIDLSLIT KETFYQIYGL LKLFDRALKL DGISSVEFQS QMELLKHSLE
TRGFTFTQYL DIFKGFARSV SNVINDYFNN IHEYNLNRII ARMSRNEILD KYRIPDGDGD
PEKLQHWISE IFLREKIALS LGIQQLDLFL SRILTTLFHQ SYKLPDSKLR LLLNYNPQRA
MTPIRNPKKS AEGIIHLGNK GNNLVKLNQL GFQTPPGFII TTEVFRSRDV IESYPPAGQN
FKDQVARHIQ LLEEQTGKRF GDPENPLLCS VRSGSSISQP GMMDTFLNVG INEEIADGIA
RQTGNTWFAW DNYRRFLQCY GMAFDLKRND FDEIMRLFKK AKEIAVKRGF TGDQMRELAL
AYQKRITAAG ITIIEDPFEQ LLLTINKVLN SWESAKAKTY RKIIGISDDW GTAVTVQAMV
YGNLSPASGS GVFFTHNPKW SEDNLRLWGD FTIGNQGEDV VAGLVTTLPI SIIQQENEMR
DTDITLETHF PEIYQALKGW ANQLIYHNGW SPQEIEFTFE SPRKADLYIL QSRNMSIRER
KKVFTFDLED AGDERVFLGS GIGVSGGAMS GRAVFSLEEI DRWRTVEPET QLILIRGDTV
PDDIQEINAA DGLMTARGGV TSHAAVVAHR LGKTCVVGCV NLVCNEAERN GLFGDVLITS
GDFVSIDGQE GLVYKGFMKI KEA
//
