(data stored in ACNUC7421 zone)

SWISSPROT: C3MHM9_SINFN

ID   C3MHM9_SINFN            Unreviewed;       896 AA.
AC   C3MHM9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|PIRNR:PIRNR000853};
DE            EC=2.7.9.1 {ECO:0000256|PIRNR:PIRNR000853};
GN   Name=ppdK {ECO:0000313|EMBL:ACP24357.1};
GN   OrderedLocusNames=NGR_c05620 {ECO:0000313|EMBL:ACP24357.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24357.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24357.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + phosphate = AMP +
CC       phosphoenolpyruvate + diphosphate.
CC       {ECO:0000256|PIRNR:PIRNR000853}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000853,
CC         ECO:0000256|PIRSR:PIRSR000853-3};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|PIRNR:PIRNR000853}.
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DR   EMBL; CP001389; ACP24357.1; -; Genomic_DNA.
DR   RefSeq; WP_012707142.1; NC_012587.1.
DR   RefSeq; YP_002825110.1; NC_012587.1.
DR   STRING; 394.NGR_c05620; -.
DR   EnsemblBacteria; ACP24357; ACP24357; NGR_c05620.
DR   GeneID; 7791788; -.
DR   KEGG; rhi:NGR_c05620; -.
DR   PATRIC; fig|394.7.peg.3378; -.
DR   eggNOG; ENOG4108HRN; Bacteria.
DR   eggNOG; COG0574; LUCA.
DR   HOGENOM; HOG000039664; -.
DR   KO; K01006; -.
DR   OMA; YRRFVQM; -.
DR   OrthoDB; POG091H09RL; -.
DR   Proteomes; UP000001054; Chromosome.
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:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.50.30.10; -; 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; IPR002192; PPDK_PEP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR22931:SF29; PTHR22931:SF29; 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; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHM9.
DR   SWISS-2DPAGE; C3MHM9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Kinase {ECO:0000313|EMBL:ACP24357.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000853-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000853-3};
KW   Pyruvate {ECO:0000313|EMBL:ACP24357.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000313|EMBL:ACP24357.1}.
FT   DOMAIN       21    297       PPDK_N. {ECO:0000259|Pfam:PF01326}.
FT   DOMAIN      315    371       PPDK_N. {ECO:0000259|Pfam:PF01326}.
FT   DOMAIN      436    516       PEP-utilizers. {ECO:0000259|Pfam:
FT                                PF00391}.
FT   DOMAIN      530    882       PEP-utilizers_C. {ECO:0000259|Pfam:
FT                                PF02896}.
FT   ACT_SITE    468    468       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000853-1}.
FT   ACT_SITE    844    844       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000853-1}.
FT   METAL       758    758       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000853-3}.
FT   METAL       782    782       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000853-3}.
FT   BINDING     574    574       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     630    630       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     758    758       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     779    779       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
FT   BINDING     780    780       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
FT   BINDING     781    781       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     782    782       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
SQ   SEQUENCE   896 AA;  97093 MW;  C6105E59E5AAD778 CRC64;
     MTKWVYTFGG GKAEGSAGDR NRLGGKGANL AEMCNLGLPV PPGLTIVTDA CNSYFDNELT
     MPEGLREQVR EGIARMEEIT GRAFGDTSHP LLLSVRSGAR ASMPGMMDTV LNLGLNDQSV
     HALGHDAGDA RFAWDSYRRF IQMYGDVVLG VDHEIFEEIL EEEKARLGHE QDPELSAVEW
     QHVISRYKEA IEEVLGEPFP QDPEVQLWGA IGAVFSSWMN PRAITYRHLH GIPAAWGTAV
     NVQAMVFGNL GNSSATGVAF TRNPSTGAKE LYGEFLVNAQ GEDVVAGIRT PQNITEAARI
     ASGSDKPSLE KLMPEGFAEF ETICQTLERH YRDMQDLEFT IERGTLWMLQ TRSGKRTAKA
     ALKIAVDMAE EGLISKEEAV ARIDPASLDQ LLHPTIDPHA RRDIIGSGLP ASPGAATGEM
     VFTSEEAVQA VKEGRKVILV RVETSPEDIH GMHAAEGILT TRGGMTSHAA VVARGMGTPC
     VSGAGNIRVD QRAELLITAS VTLKKGDVIT IDGSSGQVLK GEIAMLQPEL SGDFGKIMQW
     ADQSRRMTVR TNAETPADAR AARSFGAEGI GLCRTEHMFF EDDRINVMRE MILAEDEEGR
     RAALAKLLPM QRSDFVELFS IMHGLPVTIR LLDPPLHEFL PKTDEEIAEV AGVLSLDPAH
     LRQRVDALHE FNPMLGHRGC RLAISHPEIA EMQARAIFEA AVEAARVTGA PVVPEIMVPL
     VGLRAELDYV KERIDAVAKE VIGEAGIGID YLVGTMIELP RAALRADVIA EAADFFSFGT
     NDLTQTTFGI SRDDAAQFLA TYQQKGIIEQ DPFVSLDFDG VGELIQLAAE RGRRTKNGLK
     LGICGEHGGD PASIRFCEEA GLDYVSCSPF RVPIARLAAA QAAINGNGKT EALAAS
//

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