ID A0A1G0S8F4_9BACT Unreviewed; 734 AA.
AC A0A1G0S8F4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
DE Flags: Fragment;
GN ORFNames=A2W30_06020 {ECO:0000313|EMBL:OGU68605.1};
OS Ignavibacteria bacterium RBG_16_36_9.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798435 {ECO:0000313|EMBL:OGU68605.1, ECO:0000313|Proteomes:UP000178123};
RN [1] {ECO:0000313|EMBL:OGU68605.1, ECO:0000313|Proteomes:UP000178123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:OGU68605.1}.
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DR EMBL; MHAH01000038; OGU68605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0S8F4; -.
DR Proteomes; UP000178123; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.80.30; -; 1.
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 Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
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; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 3.
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};
KW Kinase {ECO:0000313|EMBL:OGU68605.1};
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:OGU68605.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..60
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 61..305
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 312..366
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 436..519
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 554..724
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 734
FT /evidence="ECO:0000313|EMBL:OGU68605.1"
SQ SEQUENCE 734 AA; 81485 MW; DFCF6143ACA95444 CRC64;
MPGKYVYFFG GKKAEGKAEM KSLLGGKGAN LAEMVNISLP VPAGFTITTE VCTYYYDNNK
KYPKELKAQV LAALNKVEKE MGAKFGDSEN PLLLSVRSGA RASMPGMMDT ILNLGLNDET
VQALIRKTNN PRFAYDSYRR FVQMYGDVVL GLKPVHKHDE DPFEVILDKK KHQHGFRLDT
ELTADHLKEL VEEFKAAIRE KTGYDFPSDP MDQLWGAVSA VFGSWMNERA IVYRKLNNIP
ADWGTAVNVQ SMVFGNMGED SGTGVAFTRD PASGENVFYG EYLFNAQGED VVAGTRTPHP
ISELKKEDPK IYKQLDNFRK ILENHYKEMM DIEFTIQQGK LWMLQCRVGK RTGFAAIRMA
VDMVKEKLIS KEDAIGRIEP NQLNQLLRPI FDQNEKNKAV SEGRLLAKGL NAGPGAASGK
VALSAQDAEE MAAKGDPVIL VRIETSPEDI KGMNASEGIL TARGGMTSHA ALVARQMGKV
CVAGCGSLKI NYKERTIGVE GKNDIVREGD YISIDGTTGE VIKGKLETKP SEVIQVLISQ
TMQPKDSSVY QTYSSLMKWA DEIRRLKVRT NADQPDQARN AIAFGAEGIG LCRTEHMFFG
GDRITSVRKM IVSDTVEERK AALAELLPLQ REDFEGIFEA MKGRPVTIRT LDPPLHEFLP
HSEKEIAELA ADLGIDQSKL KAKIESLHEF NPMLGFRGCR LGIVFPEITE MQARAIIEAA
VNVSMRRIPV KPEI
//
