ID   I3TVT8_TISMK            Unreviewed;       652 AA.
AC   I3TVT8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE   AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN   OrderedLocusNames=TMO_c0266 {ECO:0000313|EMBL:AFK56876.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM3 {ECO:0000313|EMBL:AFK56876.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56876.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK56876.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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DR   EMBL; CP003239; AFK56876.1; -; Genomic_DNA.
DR   RefSeq; WP_014747865.1; NC_017958.1.
DR   AlphaFoldDB; I3TVT8; -.
DR   KEGG; tmo:TMO_c0266; -.
DR   HOGENOM; CLU_420301_0_0_5; -.
DR   Proteomes; UP000005258; Plasmid pTM3.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR000121; PEP_util_C.
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; PF02896; PEP-utilizers_C; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AFK56876.1};
KW   Plasmid {ECO:0000313|EMBL:AFK56876.1};
KW   Pyruvate {ECO:0000313|EMBL:AFK56876.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Transferase {ECO:0000313|EMBL:AFK56876.1}.
FT   DOMAIN          306..634
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   652 AA;  71632 MW;  055C54FB31D7BBD6 CRC64;
     MATLSKFDFK ELLTGISTRA RRPEDILSGI RAADLEGVIF PRFSDDEYTP FASGEAIHDG
     DHSGYLVLHR STAQQISDGA GDSSDAPDYI YSVAEGDIDD FAAIKGAAGF FTNHPGKTTF
     SPVQSVSEGK STIIAANIDY HESDEPVDLH FQTKSGGSRI VRTRKRWIST VDIDGREARV
     YEGDMVAMSG SRGLVFAGAR VVAPSRIDTL YNLLTDAYLA AETEFGPASA WERLSDTAFF
     AAHREEIREI VASDEFRGFQ SLIGFCHAQS PLRVYVNVHK TACVVRARLL ASTLTFDGTG
     LSIDCNEAAL GVGLLRDERM WIDPSDIDIL RILFLGDDCT TKEHYDRIVR QYERRHGDRY
     YSIFSARPGA ICVVRTLCMP FSKFLPDNFD IADFAARHGL DPAKTQSAFR RLSGEREVYH
     GCRGIRLFSI RPDLARLWLR TVLGALARAN ADGAAVKVRF LLATLTLPDE ASRFIVTLEE
     VASSIFGSVK AAPIEGATTM LETGGAFICL ESILRQRGHE LGMVGGLIGS NDFTTACLNM
     NRSDAPRHLI PGYVEQGFFA SSPFTHVQVS VVGRAMHEAL QRSTRLALEL DQQFIWGLAG
     ELTTDWHSVQ WLARFLAPAG LTYLSTSPET IIAALLASAA TRYQRPEVSR AA
//