ID A0LLP2_SYNFM Unreviewed; 868 AA.
AC A0LLP2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Sfum_2666 {ECO:0000313|EMBL:ABK18344.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK18344.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK18344.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK18344.1; -; Genomic_DNA.
DR RefSeq; WP_011699511.1; NC_008554.1.
DR AlphaFoldDB; A0LLP2; -.
DR STRING; 335543.Sfum_2666; -.
DR KEGG; sfu:Sfum_2666; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_011040_0_0_7; -.
DR InParanoid; A0LLP2; -.
DR OrthoDB; 9760711at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001784; 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};
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:ABK18344.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK18344.1}.
FT DOMAIN 131..434
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 490..559
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 868 AA; 95611 MW; 49BEEC25D5B7302A CRC64;
MLKFFEMFRK NRLLQAESPE KAAFQYKYKH FQNLLAGNSR ALEIMTELEQ TCYGPKPFAL
DDVVDRTASL VSRVYDIVED LNALAGGAFP GLFDALERVG ESIRKELTRK KGPEETSLTI
PLQHLSLDRV SEVGGKAANL GEVYNRIHLP VPRGFAVTAH ACSLFLESND LFKRSGGILK
GLDVENTSRL LECSREIRAA IVNAVLPAEL ERCLKEEVAA LTAEFGSGIG FAVRSSATSE
DSEASFAGQH STVLGVGRDR IVQAYKEVVA STFNPRAVYY RRTKGYPDEY VIMSVLCVVM
VDAGAGGVMY TRDPNNPGRD VLMINAVWGL GVGAVDGSAA TDFFEVDKKD RRLLASHVAE
KPTRFVIGPD WKPEEQPVPE ELRSKACLNP DQLMLLAEYG LTIESHYGVP MDIEWALDSR
GRLILLQARP LNVELTGIRG EPATADQEPG SIERAVAAHA VLLRGGMTAS RGKASGFAYV
LNSDHNLLNV PEGAILIARQ TSPRYVAILG RARAIVTDVG SVTGHMAAVA REFGVPALVG
TGNATEVIGH GEEVTVDATN RMVFKGRVES ILGRKRQVNP MKGSPVYRIA HSVLKRIAVL
NLVDPKSDQF SPEGCQTLHD IIRFAHEASM REMFRISDDL DVNRSFAVRI KAPLPMKIFA
VDLGNGLSIQ RGTPEARVED VASVPFRALL QGMTRPDVRW IGPVDVNWKG FAAIVTESIF
SDPTLDDRMG GPNYVVISGE YLNFNSRLGY HFAVVDSYCG ENVNDNYITF SFKGGAADIG
RRSRRALLIT KILKRLGFKT EIKGDLVRGE LKKFQSGVIE EKLDMIGRLL GAVRLLDMVL
SDDGHIDWYV EEFFKGNYTF QRPLRQKT
//
