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Database: UniProt
Entry: F3BAR8_9FIRM
LinkDB: F3BAR8_9FIRM
Original site: F3BAR8_9FIRM 
ID   F3BAR8_9FIRM            Unreviewed;       874 AA.
AC   F3BAR8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=HMPREF9477_01038 {ECO:0000313|EMBL:EGG83277.1};
OS   Lachnospiraceae bacterium 2_1_46FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG83277.1, ECO:0000313|Proteomes:UP000018451};
RN   [1] {ECO:0000313|EMBL:EGG83277.1, ECO:0000313|Proteomes:UP000018451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG83277.1,
RC   ECO:0000313|Proteomes:UP000018451};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:EGG83277.1}.
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DR   EMBL; ADLB02000001; EGG83277.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3BAR8; -.
DR   STRING; 742723.HMPREF9477_01038; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_015345_0_2_9; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000018451; 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:EGG83277.1};
KW   Magnesium {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:EGG83277.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018451};
KW   Transferase {ECO:0000313|EMBL:EGG83277.1}.
FT   DOMAIN          17..293
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          302..354
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          421..502
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          519..869
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        454
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         560
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         616
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   874 AA;  96440 MW;  FF1284412D68FEFB CRC64;
     MAKWVYMFTE GDATMRNTLG GKGANLAEMT KLGLPVPQGF TITTDACTQY YEDGRKINDE
     IMEQIMDAIV KMEEVTGKKF GDKENPLLVS VRSGARASMP GMMDTILNLG LNEEVVKVLA
     EKSGNPRWAW DCYRRFIQMY SDVVMEVGKK YFEELIDKMK EEKGITQDVD LTAEDLEVLA
     NQFKAEYKEK IGEEFPIDPK EQLMGAVKAV FRSWDNPRAN VYRRDNDIPY SWGTAVNVQM
     MAFGNMGETS GTGVAFTRDP ATGEKHLMGE FLMNAQGEDV VAGVRTPQKI DQLKEVMPEV
     YEQFVGICNT LEDHYRDMQD MEFTIEDKKL YMLQTRNGKR TAQAALKIAC DLVDEGMITE
     EKAVAMIDPR NLDTLLHPQF DAAALKAAAP VAKALGASPG AACGKIVFTA EDAKEWAERG
     EKVVLVRLET SPEDIEGMKA AQGILTVRGG MTSHAAVVAR GMGTCCVSGC GDITMDEANK
     KFTLAGKEYH EGDSISLDGS TGNIYDGIIP TVDATIAGEF GRIMGWADKY RTLKVRTNAD
     TPADARKARE LGAEGIGLCR TEHMFFEGNR IDAFREMICS ETLEEREAAL EKILPEQQGD
     FEALYEALEG HPVTIRFLDP PLHEFVPTTE EDIKKLADTQ GKTVEQIKAI IDSLHEFNPM
     MGHRGLRLAV TYPEIAKMQT RAVIRAAINV QKAHSDWTVK PEIMIPLSCD AKELKYVKDM
     VVATADAEIA AAGVELAYEV GTMIEIPRAA LTADEIAKQA DFFCFGTNDL TQMTYGFSRD
     DAGKFLDAYY DAKIFENDPF AKLDQTGVGT LMETAIKLGK PVNPNLHVGI CGEHGGDPSS
     VEFCHKIGLD YVSCSPFRVP IARLAAAQAA INNK
//
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