ID A0A0G0AAN3_9BACT Unreviewed; 1539 AA.
AC A0A0G0AAN3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=UR43_C0004G0119 {ECO:0000313|EMBL:KKP53578.1};
OS candidate division TM6 bacterium GW2011_GWF2_33_332.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53578.1, ECO:0000313|Proteomes:UP000034634};
RN [1] {ECO:0000313|EMBL:KKP53578.1, ECO:0000313|Proteomes:UP000034634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP53578.1}.
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DR EMBL; LBPE01000004; KKP53578.1; -; Genomic_DNA.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034634; 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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..386
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 1539 AA; 172838 MW; 40D2DD932A62E596 CRC64;
MLHKKLKMLW ILILHFVASG MVKAVLDPIA LKHRAEVEGV GYKVANLEQL RSLFENKNFD
GFTILVPAFE SINSDLVKEF LSQHNLKIDL AWQELIRDSE IFANQAACDQ CFSTKKYPSR
FFEKLAELRA KIERVFDVAT TDTIQTLNYF PQMKKIKEFG KSHGTKLMVR STGKEDTDKI
ANAGGNESVA NVSPNEKTIL AAMKIVVLSY FSEKSLIQRL GAGDQAIFKE PPFIPVLLQI
MVGEKIGKSI PSCGVMFTED PESSFSRGKQ PTTGITIIQS SFGHNEGVVN SIVSVDTFYT
DSNNHIVPVM RPKYFRLVPE DEGKLQTKDN PEEIIKESSL SVEAIKALKA ISERLENYYQ
KPMDVEFVVD HETKTIFLVQ ARPITYAALL VQSCYLVDID KIPDSKKITG NCIGSAGGQL
RIIRSARNCI ISKTLPAALE QYQSSDNAKD IECILVGAMA PATSHEATTF RGESKPVLFV
KDLSILEQWI EKEKSFVVDL QQEIVIQEDG VEGLQQLIDQ GKAHAGWISY PMPRLMSVGS
FALQDTSSKP WDAVISIELH KKLADKKTQE LVYNIKTLPR DEALNSLFEL MFMIDKTVTK
AGKKVILNQA LDAEIEQFGA WVYTIANSIK SLIGYQPGSL GYILRLFSIR QLETLIYQQP
GNDIIDGFSL VTLAKTLQQE ASSQKLLLQK QKIGFPPRRP ASKIIVLQAV QYIKLKEFAL
TNELQQEWLN FVSKLTTIKD VNLQKNFNVM FAHLGRLNIL PLWQNTLFAQ TYKDKSGNAE
DVATTLSDQY SEVKIFIDQL NKISKKLESI NLNALDNPSK FEKTWNSFIN DIVKYFKSED
FLTGFNSSNQ LGKMIALHTM EQLVSKFDGA IKTVEGSANY KIVTSKDSPE YEKHSDKIFT
FKKMLERYRD LLILWTKSLQ VSELFGENEI SVQRYRLNRF DACVTIDSNN LKSSRGFDVG
SVALGSGGLR GIQPTTLEDF FTLIHQSLLN IVSGWHKKIG GEKIDLPNWI QKLKDFITIN
KFYLGMRDAL LVGVQFDPPI VSFSYNISLG NHSARIILTY NKKTNSGFLE IVMIGDQGSL
LRWNVIRDFV LVMGSFLQTG TTVSLSEKNV SGKIVLGEKS NISLIMYFLD KVIDLAEISL
EALPTVGSFL TSLPKDQQIA FAYKILKLSF EKPELIRVLS EMHTAAMKIL IENKQDISLF
VNKAVQFAKI GNPQKQAIAL SLLSAIVQEL PYYQQAFEAL NAVLLTKNPV VQEEIVRLCA
ALLGKKQIYP QIITVIANNL HSVVARNFLQ EIPLDVLDLS PIIPAAITLM QDNSKGEKIL
LMFYSLLDKG KGFPESIKVA CGALKSSNDL SKSRAVELFN KLFEYGKGFD EAEKVLNETL
LPSNEECGEP FNVKTKFFIN LVEHEKSFSK AVEYAALEFI YKLSRGNAMK IFSKLFGKGK
GFTQAANAAV EVFKLDPWNN SGQDQYDALG LFEKIFDYGY GFEQAQAVIR EIQEPTPEFY
RIAQELQEYL PQLQELIAKK QADLAARSVA LSIASTVPE
//
