ID A0A0L6U2F6_9FIRM Unreviewed; 873 AA.
AC A0A0L6U2F6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AKG39_04970 {ECO:0000313|EMBL:KNZ42691.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42691.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) 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}.
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:KNZ42691.1}.
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DR EMBL; LGYO01000010; KNZ42691.1; -; Genomic_DNA.
DR RefSeq; WP_050739265.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U2F6; -.
DR STRING; 52689.AKG39_04970; -.
DR PATRIC; fig|52689.4.peg.73; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000036873; 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; IPR023151; PEP_util_CS.
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; 2.
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; PS00742; PEP_ENZYMES_2; 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:KNZ42691.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:KNZ42691.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036873};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNZ42691.1}.
FT DOMAIN 59..291
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 303..356
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 422..503
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 518..869
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 455
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 831
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 745
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 768
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 769
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 873 AA; 96143 MW; 32F4E76F3F3AB8C1 CRC64;
MSNKWVYLFK EGNAGMKALL GGKGANLAEM SNIGLPVPQG FTVTTEACTE YYNQNMKLSD
EIRTQIDESL KIIESQTEKQ FGNKENPLLV SVRSGAKFSM PGMMDTILNL GLNDETVAGI
AKITNNERFA FDSYRRFIQM FGDVVQEISK EKFDRVLDDA KEANAYQDDT QLTAEDLKKI
VVAYKKIIKD ETGKDFPMDP KEQLLMAIEA VFRSWNNNRA ISYRNMNDIP HDIGTAVNVQ
SMVYGNMGDD SGTGVAFTRN PATGENKLYG EFLINAQGED VVAGIRTPKD INDLKDIMPD
IYQQFHDTAN LLENHYKDMQ DIEFTIEKGK LYMLQTRTGK RTAAAALCAA TEMVEEGLIT
KEEAILRLDP VSLDQLLHPT FETAALAAAE LLATGLPASP GAATGKVYFT AESVCTAVAN
GEETILVRKE TSPEDIEGMY AANGILTARG GMTSHAAVVA RGMGKCCVAG CESIKVDEAS
RQFIVGGMVF KEGDYISLNG STGKVYKGSI KTMTPELSGH FGEIMAWADE YRTLNVRTNA
DTPRDAEVAV RFGAEGIGLC RTEHMFFDEV RIPIVRRMIL ASTKAQREEA LAKILPMQKK
DFIGIYKAME GRPVTVRLLD PPLHEFLPTE EKDIAALATD IGITNDDMIA VISGLKEFNP
MLGHRGCRLA ITYPEIAEMQ TRAIMEAAIE AKEAYGFDVV PEIMIPLIGI KEELTYLDEV
VRKIAEQVKA EKKSDIKYLV GTMMEIPRAT LIADQIAETA EFFSFGTNDL TQMTYGFSRD
DAGKFITDYK EKGILKNDPF ESIDIEGVGK LVETGVTLGR QTKPDLKVGV CGEHGGDPKS
IYFFHKVGLD YVSCSPFRVP IARLAAAQAA LGK
//
