ID C7LUS7_DESBD Unreviewed; 692 AA.
AC C7LUS7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding {ECO:0000313|EMBL:ACU90992.1};
GN OrderedLocusNames=Dbac_2917 {ECO:0000313|EMBL:ACU90992.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU90992.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU90992.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(2009).
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DR EMBL; CP001629; ACU90992.1; -; Genomic_DNA.
DR RefSeq; WP_015775081.1; NC_013173.1.
DR AlphaFoldDB; C7LUS7; -.
DR STRING; 525897.Dbac_2917; -.
DR KEGG; dba:Dbac_2917; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_7; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000002216; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:ACU90992.1};
KW Pyruvate {ECO:0000313|EMBL:ACU90992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW Transferase {ECO:0000313|EMBL:ACU90992.1}.
FT DOMAIN 19..233
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 244..297
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 613..684
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 692 AA; 76207 MW; A0D2FF99A548795A CRC64;
MNILPIPVTG RDSRNLMPLS GAKAVNLRHL SLHGFAVPTT LFVPPAAYAE FVRHTGLSQH
IEAVTASLRE AMRWEEIWDV SLKLRNAFLR QPLPEPMAKA ILATVENALP GASLAVRSCS
PDEDSGFSHA GMHDSVLEVR GPEELSCAIR TVWASLWTDR AILYRREMGL KAGTSDMAVL
IQPMIYGRVS GVLFTASPVD EFTSIIESAP GLAREVVEDR VGTERIVMSR SSGAELSRTP
FLEPVLGGEE ARKLLELGLQ IERLFGAPQD IEWTLADTGP VILQARPVTT LARSSNAAGW
SDRDKRPWYL SLTRSHGNLL ELRNRIEGQI LPGMLEESER MKDVNLSAMS PAELEAEVLR
RREVLERWRD IYWRELIPFA HAVRQFGMLY NDAVAPEDPF EFTALLTGQQ LLAVRRNDLL
TELAAMVRAD AALAARLGDA DIPADGKFAE KLEEFKQDFG DLSCGTSWCE EGPQGIVRLT
LELARHEPRR RSARGAADLE ERFLAALSRE KRDFGAAVLD LARTSYRLRD DDNLYLGKIQ
ARHDEALAHA LDMGLTMDHA VREGRSSLPK GNAWTENVGS SAPGTLFKGW AASAGVARGK
ARVVTEPEDL FSFRAGEILV CDALDPNMTF VAPLAAGIVE RRGGMLVHGA IIAREYGIPC
VTGVDEATVR IKNGQTLLVD GFRGEITLEQ QD
//
