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Database: UniProt
Entry: A0A1W1V8Z2_DESTI
LinkDB: A0A1W1V8Z2_DESTI
Original site: A0A1W1V8Z2_DESTI 
ID   A0A1W1V8Z2_DESTI        Unreviewed;       885 AA.
AC   A0A1W1V8Z2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=SAMN00017405_0658 {ECO:0000313|EMBL:SMB89755.1};
OS   Desulfonispora thiosulfatigenes DSM 11270.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfonispora.
OX   NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB89755.1, ECO:0000313|Proteomes:UP000192731};
RN   [1] {ECO:0000313|EMBL:SMB89755.1, ECO:0000313|Proteomes:UP000192731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB89755.1,
RC   ECO:0000313|Proteomes:UP000192731};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FWWT01000016; SMB89755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1V8Z2; -.
DR   STRING; 656914.SAMN00017405_0658; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000192731; 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; 3.
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:SMB89755.1};
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:SMB89755.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192731};
KW   Transferase {ECO:0000313|EMBL:SMB89755.1}.
FT   DOMAIN          19..56
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          62..302
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          305..358
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          520..877
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        838
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         751
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         751
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         772
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         773
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         774
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         775
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         775
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ   SEQUENCE   885 AA;  98061 MW;  D89638CCDDF19549 CRC64;
     MKNKKYVYLF AEGSKDMRNL LGGKGANLAE MTNIGLPVPP GLTITTEACI DYFELGKKLP
     ESLEADLWDK LETVEEATGK KFGDNSNPLL VSVRSGAVAS MPGMMDTILN LGLNDETVEG
     LAKSVNDPRF AYDCYRRFIQ MFSDVVMEVE HYEFETILAK QKDTAGVKND NELSAEDLQN
     IIKEYKVLVK RSAGKEFPQN PTEQLIMAVQ AVFDSWYNPR ADYYRKINNI SDALGTAVNV
     QSMVFGNMGA KSGTGVAFTR NPANGENKLY GEYLMNAQGE DVVAGIRTPN PITNLQEDSP
     VVYDQFVKIA NLLENHYRDM QDIEFTIENE KLYMLQTRTG KRTTAAAIRI AAEMVDEKLI
     TKEEALLRIE PTQLDQLLHR SIDPNAELIV IAKGLPASPG AGSGRIVFNA DDAENLGKEG
     KDTILVRLET TPDDIHGVVY SRGILTSRGG MTSHAAVVAR GIGKPCVCGC EALEIDVVNE
     KLVVGKHQFK KGDIISIDGT TGNIILGQVP MIDPELSPSF QRILTWADEI KTLSVRANAD
     SPEEAKKARE FGAQGIGLCR TEHMFMDQAR LPIVQEMILS ETIEEREKSL RKLLSFQQED
     FYGILKAMEG LPVTVRLLDP PLHEFLPNAE SLLVDITKLK CSDGDAELLE EKEELLKKVK
     ALSENNPMLG HRGCRLGITY PEIYRMQARA IFQATAQLEK EGYNIIPEVE VPLIIGPDEL
     RLLKAEIDEV AVAVREETGV DFDYHVGTMI ELPRACLTAD EIAEYAEFFT FGTNDLTQTV
     LGFSRDDSEG KFMQEYLDYK IIEHNPFIVL DQKGVGKLLK YAVKNAREVK PNLPIGICGE
     HAGEPSSIEF SHVIGLDFVS CSPFRVPIAR LAAAQAAVNN NNQSK
//
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