ID F3NK04_9ACTN Unreviewed; 898 AA.
AC F3NK04;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN ORFNames=SGM_3468 {ECO:0000313|EMBL:EGG46415.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG46415.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG46415.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG46415.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
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:EGG46415.1}.
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DR EMBL; AEYX01000037; EGG46415.1; -; Genomic_DNA.
DR RefSeq; WP_006141237.1; NZ_AEYX01000037.1.
DR AlphaFoldDB; F3NK04; -.
DR STRING; 996637.SGM_3468; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR Proteomes; UP000003022; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
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; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:EGG46415.1};
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:EGG46415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 62..285
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 300..346
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 418..500
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 541..885
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 451
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 849
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 574
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 629
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 762
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 783
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 784
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 785
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 786
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 786
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 898 AA; 95751 MW; AEF014EE108718AE CRC64;
MVRYVYDFTE GSRDMAGLLG GKGSNLAEMT RLGLPVPPGF TVTTEACRAF LDTGGAPAGM
WGEIAERLTA IETATGRALG QPEDPLLLSV RSGARFSMPG MMETVLDIGL NDESVLGLAK
VSGNARFAWD SYRRLVQMFG STVMGVDSAR FEDSLAALKT ARGVTDDVHL SADDLAELVG
TFKELIHRES GEHFPQSPAE QLHRAVLAVF TSWNGARARL YRRREHIADD LGTAVNVQRM
VFGNLGSDSG SGVAFTRDPA TGRPGLYGDY LPDAQGEDVV AGIRNTVPLT ELERLDPGSY
ARLRAHMETL ERHYRDLCDI EFTIERGTLW MLQTRVGKRT AEAAFAIASA LADEGLVTED
EALSRVAGEQ LARLMFPRFD TSGTGAPLAR GLPASPGAAV GAVVFDSAEA VRRAATGEKV
VLVRQETTPD DLPGMIAAQA VVTSRGGKTS HAAVVARGMG KVCVCGAEEL AVDTSARRCT
TPDGTVVEEG TVVSVDGSAG VVYAGAVPLT DSAVIRFLAD GSADEDGEGV VDAVARALGR
ADAVRRLEVR ANADTPEDAA RARRFGAQGI GLCRTEHMFL GERRKLVEAM ILAPDESARE
RALAALLPLQ RRDFTGILEA MDGLPVTIRL IDPPLHEFLP DRTELAVRLA AAGARGVEPG
PHDTELLDAV NRMHEENPML GLRGVRLGLV VPGLVAMQVR AIAEAVVERT RAGGSPRAEI
MVPLVGAVEE LRIEREEVER VLAEVSRESG VPVHCPVGTM IELPRAALTA GRIAAEAEFF
SFGTNDLTQT TWGFSRDDVE AAFFSAYLDK GIFATSPFET LDRDGVGRLV RIAVEEGRAA
RPGLKIGVCG EHGGDPDSVH FFHAAGLDYV SCSPFRVPVA RLEAGRAALE GTDGGDTR
//
