ID A0A1V8M6R5_9GAMM Unreviewed; 937 AA.
AC A0A1V8M6R5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=AU255_04890 {ECO:0000313|EMBL:OQK17232.1};
OS Methyloprofundus sedimenti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloprofundus.
OX NCBI_TaxID=1420851 {ECO:0000313|EMBL:OQK17232.1, ECO:0000313|Proteomes:UP000191980};
RN [1] {ECO:0000313|EMBL:OQK17232.1, ECO:0000313|Proteomes:UP000191980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|EMBL:OQK17232.1,
RC ECO:0000313|Proteomes:UP000191980};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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}.
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:OQK17232.1}.
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DR EMBL; LPUF01000001; OQK17232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8M6R5; -.
DR STRING; 1420851.AU255_04890; -.
DR OrthoDB; 1108665at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000191980; Unassembled WGS sequence.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191980};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 468..520
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 586..909
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 937 AA; 105178 MW; 5AB9C218E32BF6F5 CRC64;
MKESPKGPFI RVFWFCNDGE ILLPKPYACT EHGGGYQHGK LNDRALILRN NGYWIANLLA
GIDTKNILAS DDFVDWYGQL LIEKFLIRTD NGWILKKALY YRGAIQEEDE RYGARMLLTA
LAEKNEWIKR RYSALRTGVQ LLPHGEDSAS IQKVRQMSVS LAEQDEQFVN LRTKIHVSPD
AGDARLVREY AAKISDPQQQ AKYMELAQEI DRVFQSHPLH QLLERNAKIF SAEPWLQQLL
LEAGKAYHSD NSAGNYYAVT SHLLADLRDA LPKIRKPGSR LRILDLSLAV EVENFRVSTQ
LKSTLTKVNR LQRISWLRDA ALAAYGTGHI NHRSLEALQA SISRMEYAQL PLTTYFNELK
YLSRAPGWST QELRFQFYQS MIKLTEIEPL AIFFIQDILR GSPMLFFSQI LDSLSRDANQ
LAGTTHKIFN TQVGVGFHAL NPGLARGKLY TKVDINNSAN FDSQGIYLLP ETVADLPSIA
GIITVGEGNS LSHIQLLARN LGIPNITVNE NLLQQLQDHD GETIVMAVSP DGLIEINGDS
EYWQKFFNSN SNQQQAVIRP DLEKLDLSIQ EIIGLNSLRA SDSGRIVGPK AAKLGELYYH
YPGKVAKGFA IPFGVFRKTV LDAPYKKTEQ TVFEWMESQY AIIHALPIDS EQRKQMTESY
RAEIYDIIIN TDIGDQNRNN IRKAMINTFG STEAGVFIRS DTNVEDLPGF TGAGLNLTLF
NIVSIENIFK GITKVWASPF TARAFSWRQS LMESPQHVYP SILLMQTVAN DKSGVMITED
IDTNKKGVLY IATNEGVGGA VDGQSAESLR IDTRDGKVLL LATASAPFRK VPLPEGGIAN
VPVSDSESVL KANEISQLIQ FAKELPDTFP PITDENNNPV PADIEFGFFN GKLQLFQLRP
FLQSNKVQAS SYLMNMDKAL QNNMNRMVLM NEVPEEL
//
