ID A0LJZ4_SYNFM Unreviewed; 1424 AA.
AC A0LJZ4;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Pyruvate phosphate dikinase {ECO:0000313|EMBL:ABK17746.1};
DE EC=2.7.9.1 {ECO:0000313|EMBL:ABK17746.1};
GN OrderedLocusNames=Sfum_2063 {ECO:0000313|EMBL:ABK17746.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK17746.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK17746.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000478; ABK17746.1; -; Genomic_DNA.
DR STRING; 335543.Sfum_2063; -.
DR KEGG; sfu:Sfum_2063; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_257090_0_0_7; -.
DR InParanoid; A0LJZ4; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000001784; Chromosome.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK17746.1};
KW Pyruvate {ECO:0000313|EMBL:ABK17746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000313|EMBL:ABK17746.1}.
FT DOMAIN 976..1204
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 1329..1408
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 1424 AA; 163307 MW; 508D14A675C53E5A CRC64;
MQIKDTNSME YEIQSDALTK NMDITKVAVD VPSLFEILRE AVKGYAGKEQ QARELLVEYH
HRYRNWTFVI QETKRYAISN LRLYHRHPLN GGVIFLLSDI LLEALKQSER FEVRSLAADH
LLDFWFKLLD EMPEEIARPL PDGLAVDDVG RAIETHAACH QGVLRYFFKQ LAGLPEAPFE
HLMRCFYQPK RLAARLLKIW SEPASFEEIR ALLRRLHEET YLFWVSKEDP CGWLAEQGGG
PLPTCVELCR PLGHEQYLEY MRVLRTEIDP EPDHLQATAA LAGLTDYHDI VRLYFRLPDK
LKSCEIPLDG TPLSLLMRLK IIEVRGLEGI HEETLREINF EIARWIHQKP VEGLQSFLER
IFDVLGHCLL NYPEAALQIV RTIGLEILET NDRQLINFFL RHIIRMGFQT PQLGGVSEHW
QIEVNPAHLP NIRIWLEIIK KNPERTGLLL SALIVNLFLG GIYIRDTDLF QKDVSLLLHS
PIRPVYNMIK QLAKIFPVYF NQIGAEGLLR TVSTDVDELT GRSDRLIHFL RKQSHVESNN
IVVTFIQAII EFWRTLDKSR LLELVPPEVY PEIATSGPLV EEIHRIFVSI FESRTIHHAP
DLLDLTEEGT RELIWAVPEV SERERRRAFL MIQFYQLLHE KYALSFKDIE VHLQRAANLG
LPDPGALLKA LGSTDTYVKL EAILEYLLEL KEVILTSREL NVLENIYIKR HIAVDIPSMY
GSYNETKFDA LGLTFRLENL ANVLFEEIIL SFNLGFITRA TFFRIAKFLP LFMKALEIDG
ISSNHLEQQK ELFLKALAIP RFSHSQYMDL FKGFSEAIKQ VIQANYHNLH EENLETVIKW
LGRDRLLSRY RRDTGDESAA ERNQRISESF LRDLIARTFG LQYFDHFITS ILTTLATQRE
ELSVDKLDLL LSYDQERTTS YIYEPNARTF DLIHLGNKGY TLAKLHSIGI RVPPAFVITT
EYFRCRSVID GFTHSNVDFQ DRVMSHVRRL EEQTGRSFGV PGNSLLLSVR SGSAVSMPGM
MNTFLNVGIN EDIVEGLIRQ TGEGWFAWDN YRRFIQSWAM SFGMQRDEFD GIMNHFKRLY
GRQVKREFTP QEIKELALAY KEALKSHRID FSDSPREQLF TAIRMVMKSW NSPKAVTYRE
IMGLSENWGT AVTIQAMVFG NLDNQSGAGV MFTHNPWTAE SHVDPVGDFT LGNQGEDVVG
GLVKTLPLSE KQRMTQGERK DFSLEMLFPK VYQRLVEIAK ELIYGQHWSP QEIEFTFQGA
EGDGLFVLQS RNMAPRVKRD YPVFKPSEDL HAGYVGSGIG VSGGALSGMV AFDLETIQRL
RREHEGRPII LIRSDTVPDD IREISISDGI LTGKGGATSH AAIVAHRLGK ICVVGFSKMK
VWEAERKCVV DGHELHTGDF IGIDGRSGAI YVGEHATEHV EVVN
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