UniProt: A2SP39

Database: UniProt
Entry: A2SP39_METPP

LinkDB:  A2SP39_METPP 
Original site:  A2SP39_METPP

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   A2SP39_METPP            Unreviewed;       856 AA.
AC   A2SP39;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   SubName: Full=Pyruvate phosphate dikinase {ECO:0000313|EMBL:ABM97328.1};
DE            EC=2.7.9.1 {ECO:0000313|EMBL:ABM97328.1};
GN   OrderedLocusNames=Mpe_B0560 {ECO:0000313|EMBL:ABM97328.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OG   Plasmid RPME01 {ECO:0000313|EMBL:ABM97328.1,
OG   ECO:0000313|Proteomes:UP000000366}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM97328.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM97328.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RC   PLASMID=RPME01 {ECO:0000313|EMBL:ABM97328.1,
RC   ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000556; ABM97328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2SP39; -.
DR   KEGG; mpt:Mpe_B0560; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_015345_0_2_4; -.
DR   Proteomes; UP000000366; Plasmid RPME01.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; 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; 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   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 2.
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   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABM97328.1};
KW   Plasmid {ECO:0000313|EMBL:ABM97328.1};
KW   Pyruvate {ECO:0000313|EMBL:ABM97328.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW   Transferase {ECO:0000313|EMBL:ABM97328.1}.
FT   DOMAIN          73..296
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          309..361
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          432..513
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   856 AA;  91138 MW;  C7B31F6CFE0EA1C0 CRC64;
     MPRTFRIKGR HESMTSVTAA ERFVYSFAEA THLDAAALGG KGAGLVQMTA AGFPVPPGFV
     ISTQACRVSK DGAVPEALWR EIVQAVHQLE ERTGCGFGKG PRPLLVSVRS GAPVSMPGMM
     DTVLNLGMNE ETTVALAKAT GGRYRFAAET FARFARMFAD IVLGAADESA ADGASLDTVE
     DERSLRSAVR LVAEGVGASG TFPADPWAQL RQAVVAVFES WNSRRAIRYR DHHGIAHDLG
     TAVVVQQMVF GNLGSPSGTG VAFTRDPRDG SPKLFGEYLE NGQGEDIVAG THTPESLDDV
     GRRYPELIGQ FHSLARSLEK TYRDVLDIEF TVQEGVLYLL QVRPGKRTAE AAIRIAGDLY
     KEGLVDRETV LQRVTADHLR QVLRPRFLVE AVEAARAGGA RLAQGTGASP GQVSGRIVFD
     PDRAEQVASG GDPVVLMRLF TSPRDLHGML AARGIVTARG GSTSHAAVVA RALDKPCIVG
     CESLDIDAER RVVRVADREL PEGTLVSLDG STGEVFEGTL STGALSTDSV SHIGAILGLA
     DDLSGCTVFN RVSTPDMARQ AIAAGAHAIG TRIDETLAAT AGFETLVDAV SAYKRGVTSA
     DSNSNALAAL EEVIAEALTD VMRAVYPKPF AARIANLSSG VAGEAVSDFT DVAPSPAIWL
     PLGSPQLLRA QIRGLVRAKE TTGYPDNVIL MVGGINTEAE AIALRAACRE AGGAKLRLGV
     AARSPHGLLE LPRIARHVDM AWIDYRSLCA AIYRYPDDLM LAQDAWKSYI ADGFMPLDPA
     NEVDEAIKLL MPTLTPDTHA CEFGVTFYGW GVSEKVVRFF TERGFRNFGV EMNGLAATRL
     LLGRLASQEG AFGPPA
//

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