ID A0A1N7K094_9RHOB Unreviewed; 854 AA.
AC A0A1N7K094;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN05421774_101147 {ECO:0000313|EMBL:SIS55000.1};
OS Gemmobacter megaterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIS55000.1, ECO:0000313|Proteomes:UP000186141};
RN [1] {ECO:0000313|EMBL:SIS55000.1, ECO:0000313|Proteomes:UP000186141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26375 {ECO:0000313|EMBL:SIS55000.1,
RC ECO:0000313|Proteomes:UP000186141};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FTOT01000001; SIS55000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7K094; -.
DR STRING; 1086013.SAMN05421774_101147; -.
DR Proteomes; UP000186141; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; 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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SIS55000.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3}; Pyruvate {ECO:0000313|EMBL:SIS55000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 391..473
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 490..838
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 424
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 800
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 531
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 587
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 714
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 735
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 736
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 737
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 738
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 854 AA; 92119 MW; 3E43509D5069C69B CRC64;
MQKHPDHTPI TPTAAIAATT HGWRAKCLQR LVRLDLPVPR TVALSFSAVR SIAAGQPAPA
AAILTAFDAA PLVSIRPSPE NPDWGGPGTI LNIGLNAERH RLLASSHGHE VADALYLRFV
QAYAIHVARL DPDMFDVSAP SAEALRTALR AYEQETDEPF PQDPAVQLTQ ALRSMARAWE
GTTARLLRQA KGAPADAALG LVVQEMALGM GHGVSGSGVI QFVDPTTGLP QVTGRYLSQS
LGRDALARAA EGTIYLARDP RGPSLEELAP EAFTALIHHG IVCRRRLREE MQIEFTLEDG
ALKVLDAIKV TRSSRATLKI AVALAEDDII GKDEAVLRVE PRALSELLHP QVDPRGARDV
VVRGIAASPG AAVGRLVFSS AAAQASAARG EGCILVRRET SPEDIRGMHA AQGVLTERGG
MTSHAAVIAR GLGLPCVVGA SSMQLDARER RLIAPGGRIL REGDLVTLDG TAGEALAGAA
DMLAPALDDD FRKFLGWADS FRDIGVRANA DTPEDAQVAR DFAAEGIGLC RTEHMFFESD
RLIVMRQMIF ADDAKDRASA LTRLLPMQRE DFIHLFEIMA GLPVCIRLFD PPLHEFLPHT
REGMRELAEA LDKPLSDITR RAEALSEFNP MLGMRGVRLG IVLPEIYEMQ AQAIFEATLA
VGARGIKVEP EIMIPLVSAM REVELVKTRI DAVAAAVRTK RTVQFGYKLG VMVETPRAAL
RAGDIAQHAA FLSFGTNDLT QMTYGLSRDD AGRFMSAYVN QGVFPEDPFH MLDIDGVGEL
LLIGADRGRA TRPDLTLSIC GEHGGNPESI AFCRKAGFNY VSCSPYRVPL ARLAAAHLAL
ADRETPLDGE ETLR
//
