ID A0A1I1ABW8_9CLOT Unreviewed; 673 AA.
AC A0A1I1ABW8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SFB35484.1};
GN ORFNames=SAMN04488528_103317 {ECO:0000313|EMBL:SFB35484.1};
OS Clostridium frigidicarnis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84698 {ECO:0000313|EMBL:SFB35484.1, ECO:0000313|Proteomes:UP000198619};
RN [1] {ECO:0000313|EMBL:SFB35484.1, ECO:0000313|Proteomes:UP000198619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12271 {ECO:0000313|EMBL:SFB35484.1,
RC ECO:0000313|Proteomes:UP000198619};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOKI01000033; SFB35484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1ABW8; -.
DR STRING; 84698.SAMN04488528_103317; -.
DR Proteomes; UP000198619; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SFB35484.1};
KW Pyruvate {ECO:0000313|EMBL:SFB35484.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198619};
KW Transferase {ECO:0000313|EMBL:SFB35484.1}.
FT DOMAIN 17..281
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 673 AA; 79173 MW; DA4DF080A40C9CC6 CRC64;
MFKTISELSF KDKGKYGQKA SALGELKSNG FKVPEGFAIS NEVFMEYMRY NKIPFSLEEC
LARSEEMSEK IINGKFPIGI ENKVKELVNN INKNKLNTKY VVRSSASCED NKEHSMAGMF
SSFIDLNSFK DILRFIKKCY ASAFNDKVVA YVINNNLDIE SLKMGVVVQE FIIGEYSGVN
FSVDTIDMKE DYMHINVAKG ICDGFVSGKT DSNFFSIYKK DGSIVESKVQ DNHKTISLEN
IKKLYEITLN IEKFMKQKVD IEWTINKNII YILQTRPITT FKIREFPISW CKTGDDNYTW
YCENNEPLFP LMNEISKREV QALNKDAYDV GDESRYMDFI IQNGYSYYRN MEMLNNEERQ
KKFRAQLNQI TKEEKNIFQD IIFPSLFEMA NELDSYVEED KSQESVSDFL EKSLKYMEFT
SENHLKSTYA CEYVKEFEIY CKYIIKELSQ QDFYDLVFNK SFLTKEREYY MLMAEFINSN
NKIKSLFEKT RYNEIIYEHL KTIPDAGKFL KVMNDYIKDY GTTHLECDII SSFIEPTIME
KPARVLKYIK GFIGIEQKVY FDSIKKSQEN KERVKTLFLK KLDKAKGEEF LIKLKLAEIS
YLSRDNHHYY FERKSNAYLS LAITAASEIL KNNKIINKKE DIYFLKFDEI KKGLLYNSDF
ISLVEERKAE YEN
//