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
//