ID A0A0G1HX33_9BACT Unreviewed; 758 AA.
AC A0A0G1HX33;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=UW44_C0011G0011 {ECO:0000313|EMBL:KKT51500.1};
OS Candidatus Collierbacteria bacterium GW2011_GWB2_44_22.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618387 {ECO:0000313|EMBL:KKT51500.1, ECO:0000313|Proteomes:UP000034006};
RN [1] {ECO:0000313|EMBL:KKT51500.1, ECO:0000313|Proteomes:UP000034006}
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 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}.
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:KKT51500.1}.
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DR EMBL; LCIH01000011; KKT51500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1HX33; -.
DR STRING; 1618387.UW44_C0011G0011; -.
DR PATRIC; fig|1618387.3.peg.888; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034006; 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; 3.20.20.60; 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}; Pyruvate {ECO:0000313|EMBL:KKT51500.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 20..331
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 368..440
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 456..753
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 758 AA; 83967 MW; 191DE5C2045BC6B9 CRC64;
MSQQPALVLP FSKIRKEDIP LVGGKGANLG EMYSFGIPVP NGFVVTADAY KYVIDHNALQ
PVIREIIRQT DVNNQKELQK ASIKIQRFIN TANIPPELTS EIFDSYAGLK PGEKNPLVAV
RSSATAEDLP DASFAGQQES YLDIKGESNV LQAVRKAWAS LWGARAIFYR ATKNYDHFKV
QLAVPIQLMI QSEVSGVVFS VNPVSRNKNQ VVVEAVWGLG DYMVQGVVNP DHYIVNKDTM
TIHSRQFVPQ TIMEIMQYPS GVKRVNVPKD KINLRKLTDE QVIEVAKLSA KVHQHYFFPQ
DSEFAVENGK IYLVQTRPIT TLDMGKGAKH ISEEQILKLP QILQGEPASF GIGFGKVVKI
KTASEINKVK EGDVLVTEMT SPDFVPAMKR AAAIVTDKGG QTSHAAIVSR ELGIPAVVGT
KIATKTLKDD QIITVNGSTG TIYNGVPEKG KTVEQKDFKE AEFPKTATHV YVNLGEPDLA
PVVAQGNSDG VGLLRAEFMM AQIGVHPKKM IHDGKEKIFI EKLAESLARF TYSFGDRPIV
YRASDFKTNE YRNLVGGQAY EPIEPNPMLG FRGAYRYISD ESVFNLELEA IKKVRNKMGY
KNLHLMVPFV RTVDELIKVK RIVSASGLTR SNTFKLWMMV EIPSNVILLE DFIQVGIDGV
SIGSNDLTML ILGTDRDNET VAPEFDERNP AVTWALERVV KTANKHHITS SLCGQAASLY
PDLVEKLVGW GITSVSVSPD AVDNTRRVIA QIEKRLIK
//
