ID W0RQ30_9BACT Unreviewed; 794 AA.
AC W0RQ30;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=J421_5052 {ECO:0000313|EMBL:AHG92587.1};
OS Gemmatirosa kalamazoonensis.
OG Plasmid 1 {ECO:0000313|EMBL:AHG92587.1, ECO:0000313|Proteomes:UP000019151}.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG92587.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG92587.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG92587.1,
RC ECO:0000313|Proteomes:UP000019151};
RC PLASMID=Plasmid 1 {ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC ECO:0000256|PIRNR:PIRNR000854}.
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 ECO:0000256|PIRNR:PIRNR000854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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DR EMBL; CP007129; AHG92587.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RQ30; -.
DR KEGG; gba:J421_5052; -.
DR PATRIC; fig|861299.3.peg.5105; -.
DR HOGENOM; CLU_007308_6_2_0; -.
DR InParanoid; W0RQ30; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000019151; Plasmid 1.
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; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01418; PEP_synth; 1.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PIRSF; PIRSF000854; PEP_synthase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000854};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000854};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000854}; Plasmid {ECO:0000313|EMBL:AHG92587.1};
KW Pyruvate {ECO:0000313|EMBL:AHG92587.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 39..348
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 384..454
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 486..772
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 794 AA; 84901 MW; 34B46E71A955BF60 CRC64;
MSAIAVAPTE RLDAATVPSP SASPSYIRWF RDLSRDDVAL VGGKGANLGE MTRAGLPVPP
GFVVTVAAYE RFAGANDIAA QVSARLARTD VDDTDQLRAA SLALQKLVRE APTPDDVRGA
ILDAYGALAP LGNDGTTLVA VRSSGTVEDS AQFSFAGMFQ STLNVRGADA LLRAVKECWT
SAFTERLIFY RAKQHLTAPV LVAAVVQRMV NADRSGVMFT ANPATNDRTR VVIEGAFGLG
EVVVLGEVTP DHYEVDKQGL AVVERDVARK EFMLTRDAAS GETVRVALDE VKGREPVLSN
AEVRALTELA LADEAHYGAP QDAEWAIEDG RIWLVQTRPI TTLTEKPEGH GTGAELVHGL
GASPGTASGP ARVLGSPDEG GALRAGEVLV AAMTSPDWVP VMRRAAAVVT DAGGMTSHAA
IVSRELGIPC VVGTRSATRA LHTGQVVTVD GRLGTVVDGA PETAAAPAAL PNATAAVEPR
AGGIVTATRI YVNLGEPDLA ERVACLDVDG VGLLRAEFML LAALDRTHPR VLLRDGRGDE
LVTRMAAALE RFASAFAPRP VIYRATDFRT NEFRGLAGGD AFEPHEENPM IGYRGCFRYT
REPDLFALEL KAIARVRSRW PNLHLMIPFV RTGSELRACK HVVDASGLTD DPRFRLWVMA
EVPSVVSWLE EYVRLGVTGV SIGSNDLTQL VLGVDRDSEL VAPLYDERDR AVQDAIRAIV
RECRRLGITC SICGQAPSVH PEYAEFLVRA GVDSISVNPD AVDATRRNVA AAEQRLLLDA
ARRDAGPTFD RRSP
//
