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Database: UniProt
Entry: A5N8R5_CLOK5
LinkDB: A5N8R5_CLOK5
Original site: A5N8R5_CLOK5 
ID   A5N8R5_CLOK5            Unreviewed;       772 AA.
AC   A5N8R5;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Phosphoenolpyruvate synthase-related protein {ECO:0000313|EMBL:EDK33696.1};
GN   OrderedLocusNames=CKL_1654 {ECO:0000313|EMBL:EDK33696.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33696.1, ECO:0000313|Proteomes:UP000002411};
RN   [1] {ECO:0000313|EMBL:EDK33696.1, ECO:0000313|Proteomes:UP000002411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC   {ECO:0000313|Proteomes:UP000002411};
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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DR   EMBL; CP000673; EDK33696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5N8R5; -.
DR   STRING; 431943.CKL_1654; -.
DR   KEGG; ckl:CKL_1654; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG3848; Bacteria.
DR   HOGENOM; CLU_005950_0_0_9; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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   PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 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; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:EDK33696.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT   DOMAIN          66..182
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          191..237
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          691..763
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   772 AA;  86712 MW;  1D411ACCA2B188A0 CRC64;
     MLDMVKSFKE LTPELEKFAG GKGYMLSKMF QEGYPVPEGF VILPAAFQEG KVSSEAWNKI
     QYYLNALKEK RGKASFAGEF ETVLNVKTYE EIKNAIDIVF KSTQTERVKV YSSIQGIDRS
     HQIAVVVQLM VQSEISGVLF TADPITGSHV NMVGNFVYGL GEKLVSGESN AQIFTLKRPK
     GKYEGPTDLK KYASKLYKYS SSLHIKYKAP QDIEWAVEGG KLYILQTRPI TTLKTSNLDT
     YEWNDSLDGD YIWTNNNVGE AMSDVFTPLS WSIIRDLDEE QTPIPGYYLF SGNIYGRAYT
     NISYALSIYP AFGKSIKSLM GIMSEVFGQM PERVEIPIYP FSKLGLIKQM FPTIGHRLKK
     IIESSSKIPD HLKDSPKWCI NMRKRIGEIK SREELYNLWK KELLPYNFKA LWIALAGGRK
     MVLANKLKNE LVNLVGIEDT NILMSNFREN SSLESLGPIV GISKIIRGEM SRDEYKIQYG
     HRGPHEFELS IPDSLEDESW LNNQIEEFKK SNTNVEGLLN KQKTEYENAL KELKKRFPRK
     VRSIEKKMIK ANKAARLRES VRSEWTRAFR VNRAFALKAG ELTGIGDNVF FLYIDEVLNL
     LLGDDSKVKH ITARKNNYNK YKKLPPLPSI IRGTFNAFSW LQNPNRRSDY YDSNAAAADQ
     SAPEALKGFA GAAGKVEGIV RIIINPEDGE KFKTGEILVA ATTNVGWTPL FPRAAAIITD
     IGAPLSHAAI VARELGIPAV VGCGNATARL NTGDRVIVDG GHGIVQIVSE ND
//
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