ID A0A0S7ZGM1_9SPIR Unreviewed; 868 AA.
AC A0A0S7ZGM1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN ORFNames=AMS17_13305 {ECO:0000313|EMBL:KPJ86248.1};
OS Spirochaetes bacterium DG_61.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ86248.1, ECO:0000313|Proteomes:UP000050987};
RN [1] {ECO:0000313|EMBL:KPJ86248.1, ECO:0000313|Proteomes:UP000050987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_61 {ECO:0000313|EMBL:KPJ86248.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
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:KPJ86248.1}.
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DR EMBL; LJNB01000198; KPJ86248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZGM1; -.
DR PATRIC; fig|1704237.3.peg.1076; -.
DR Proteomes; UP000050987; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
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; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
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 PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 401..447
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 506..864
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 433
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 825
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 541
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 597
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 740
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 740
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 761
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 762
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 763
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 764
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 764
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 868 AA; 97747 MW; 1BBA0E016870B52B CRC64;
MKKYHSFSST EHIEDKDTLE LIGIRGKRVM ELATLGAPIL PGFMLPNETV NDLITKPADA
KKFLIEPLAK MERLLGKRFN DEKNPMLVKV VESPQLNMIT AFSIHNIGLC EKTVGGFATF
VGDEFAYHEY RNVLLKLTEL ERKCDIDRER IKKLEAFEKS LKVSKKQNKI REVVEENKGL
FPREVFSNAY DQLFYIIERF GTFFKSSSSN IDSAILIQAM TFGNYGEESY FGSYYTRNII
TGENEISGKY FLNAFDATET AGKPITQIDK AFLTDLKRIA GEMEKLFKEV RQIRFTVENG
RLWVIDQVPV PNKSTQSEIK TLLDLYAQKV VNDAYVINSI KPGRLSEILH PVIDLESAEK
LPKIEGGIAG AVGSAIGRVF LSTEKLLKAY KRATQTNQDT NFILAMPATF AEDVKAIEVA
KGVLSSEGGY ASHAPVVARS LGKVSLVYPD IRFSDNSMKI GNRTVKEGDY ITLNVPYYET
PSILFGKVSL IEPSPEGSGL LEFLELVQKH IDDFDVHANA DQPKDAQLAK LFKAAGIGLC
RTEHMFFHEK RINTFRAMII AGDKKERLKA LDELKEMQVA DFYKLFKIME GLPVTIRLLD
APLHEFLPHT KESMAQFIKF MKAKYPKLEE SEIRLRCDML KEFNPMLGHR GIRVAISYPE
IYNMQTRAIF EAAYSLKKEG VKAIPEIMIP IVMSAIELKT IRNGKKIEGA AIIGIKDIEK
KVRESFKSDP IEYRVGTMIE LPAAALAADK IAQYADFFSF GTNDLTQTTN GISRDDFNSF
FSDYNEFDLL EQNPFKVLGE QVKELILLAA ERGKLTRPDI AMGLCGEHGA EPENIPFVRD
VGLNYVSCSP YGIPIAKLAI AQLNLQNQ
//
