ID B8DQL1_DESVM Unreviewed; 861 AA.
AC B8DQL1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=DvMF_2187 {ECO:0000313|EMBL:ACL09130.1};
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL09130.1};
RN [1] {ECO:0000313|EMBL:ACL09130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL09130.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001197; ACL09130.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DQL1; -.
DR STRING; 883.DvMF_2187; -.
DR KEGG; dvm:DvMF_2187; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_011040_0_0_7; -.
DR OrthoDB; 9760711at2; -.
DR UniPathway; UPA00138; -.
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:ACL09130.1};
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:ACL09130.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 128..419
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 481..552
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 421..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 93645 MW; 988CD8B2EC0798FC CRC64;
MAIGELFRHW TYQVFAPGTL LRRKYNAFRE LLRHDSRSLE LIAELEDIHY GNEKVDWSRV
VELADQLDDA VRAMLGQLME MNPARYMGLA DYCNKIAFYM RMAVSVPEPD LAPPYVIPLA
EAHLRPDRAG GKAARLAAVR SQSMLPVPDA TVVTAAAYHY FIEHNELREP IDARLRRLRL
SRPDELAAIS EELRAMILEA ELPPRLEEDI LTAAYAMSPQ RTPLAVRSSA VAEDGPVSFA
GQYASVLGVE PGHAGMAWKR VVASKYQPRA LSYRILHGLA DAETPMAALL MPMLDAACAG
VIYTRDPDPP RRLPAEELTE GVTAVHAVAG TGDVLVSGDT PAQSAWLSRR PRSRILERPE
AVVATLAQPV PSTPLLTTED MKRLARYGRE LENLFGEPQD VEWVLDTAGR IFIVQSRPVP
GGTEHGIVPE QTAGAEGGPD GTAPASHGSL PLLAEGSEPV SAGVGSGTAR HAAICCEIGD
MPQGTVLVTT TLGPSLTRII DRLEAVVAQT GSRACHFASV AREFGLPVVT GIADPFTAIP
DGTMVTVDGA TGRVHAGRPP QEKGDGTRPR ARRKAAAAAR ERRGGMRRLA RAMQHIAKLN
LTDPASSDFA PENCRSMHDL VRFAHERGVA EMFSLVGRGG RGLGGAKKLR TDVPMIMYVL
NIEDGLFPTA AGKEEIGPDD FRSTPMWALW FGLSAARELW ANMPPAADWN ELDRISAGIF
RRDAPQLASY AVISAHYAHL MMRFGYHFAL VDTLCSPEDR TNYIQFRFKG GGAAAEGREL
RIRVLERVLA RQGFAVKTRG DLLDARHGPD AEAVIQKRLA MLGMLLAETR LLDVRLGDAD
EAEAMADDFL ARLDTAGEGA P
//
