ID C7LNG1_DESBD Unreviewed; 830 AA.
AC C7LNG1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN OrderedLocusNames=Dbac_2044 {ECO:0000313|EMBL:ACU90130.1};
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:ACU90130.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU90130.1, 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).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; CP001629; ACU90130.1; -; Genomic_DNA.
DR RefSeq; WP_015774221.1; NC_013173.1.
DR AlphaFoldDB; C7LNG1; -.
DR STRING; 525897.Dbac_2044; -.
DR KEGG; dba:Dbac_2044; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_011040_0_0_7; -.
DR OrthoDB; 9760711at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002216; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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; 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; IPR006319; PEP_synth.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACU90130.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:ACU90130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 127..432
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 476..545
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 830 AA; 90678 MW; 700DEC10F7CAA403 CRC64;
MTERTATKLS GNAPDARQKL EQKYQFFKNL LSRNNIVLEQ MTSLERMIHE GGSFTREEAV
TLVEAMAEHC RHLAQDVNAL CDGQFPELFE SIETAAGNAL NALNRQRTFD FSTLILPLEE
ITLEHLEEVG GKAANLGEIR NKIGLPTPSG FAVTASAAAL FLEQTDLLDT LRHQLAAMDL
SDIAALEKVC AKASERIMTA PLPPALEQGL MDKTREIINR FGPKVRLAVR SSAVCEDSDA
SFAGQHASVL GAAPATLSRA WSAVVASAFT ARAVFYRRTK GYSEQDVMMS VLVLTMIESK
ASGVLYTIDP NSAHSDDLLL AAAWGLGVSV VDGSMDVDFW RVRREDKQIL VTHVADKKSE
FVVLAQGGIV SRPVQETLRE QPCLTPTQVD ILADYALRLE AHYGMPMDIE WALDEKDQLI
ILQARPLQRA DGLNQAECCK LVPGRAPLLF GGQTASPGAA SGPVYIVQPD HELSAVPQGA
ILVARQTSPT YVAAMGKVAG IITDVGSPNG HMASVAREFG IPTLVGAGTG TALLTHGMEI
TLDATNQVVY AGQVAEILSK RKPVNLMKGS PVYKSLQEAM KFINPLHLVD PQLPEFSAQG
CRSLHDIIRF AHEMAMQEMF RLSDGLSPHT GVARELRAVL PFRVLLVDLG GGITSKAASS
WVELADLRCA PLIALLQGMG HPRIPKFAGR TQENQPPPTC YAVVSDTYVN LSGRLGNHFA
TIDSYSGPVI NDNYITFSFK GGAAQYEQRV RRTLVLAGIL RRQGFRVTQS ADSLRAEIRK
YDQRRFLERL DMLGRLLAAV RALDWRLDDD SEIARYVDAF MNGDYAFSHQ
//
