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Database: UniProt
Entry: A0A1I6NU70_9PSEU
LinkDB: A0A1I6NU70_9PSEU
Original site: A0A1I6NU70_9PSEU 
ID   A0A1I6NU70_9PSEU        Unreviewed;       808 AA.
AC   A0A1I6NU70;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyruvate, water dikinase {ECO:0000313|EMBL:SFS31409.1};
GN   ORFNames=SAMN05660874_00118 {ECO:0000313|EMBL:SFS31409.1};
OS   Saccharopolyspora flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS31409.1, ECO:0000313|Proteomes:UP000198852};
RN   [1] {ECO:0000313|EMBL:SFS31409.1, ECO:0000313|Proteomes:UP000198852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS31409.1,
RC   ECO:0000313|Proteomes:UP000198852};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOZX01000001; SFS31409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6NU70; -.
DR   STRING; 95161.SAMN05660874_00118; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000198852; 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; 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   Kinase {ECO:0000313|EMBL:SFS31409.1};
KW   Pyruvate {ECO:0000313|EMBL:SFS31409.1};
KW   Transferase {ECO:0000313|EMBL:SFS31409.1}.
FT   DOMAIN          56..189
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          195..243
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          732..803
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   REGION          694..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  87955 MW;  45BA0D3387C37811 CRC64;
     MTGDDAVVEL AQVDAGRIEL VGGKAAGLGE LVKAGFRVPE GFCLTTRAHA AGELPEQQVL
     DAYRRLGGGP VAVRSSATAE DLPEASFAGQ QDTFLNVSGE QELLSAIRRC WDSLHSERAV
     AYRAANGFTA EARMAVVVQR MVDAKVAGVL FTANPLTGTR SEMVVDAAPG LGDVVVDGSV
     IADHYVLDGT PPRTDGCLDR EQLDALREAG ARVQEEFGSP QDIEWAIDQD GELWLLQSRA
     VTTLFPLPPR TDDLRAYFEM GHMQGMTRPF TPAGMSAMTH GAQQWMESAG LAGGAFGDAM
     GITPVGGRLF MDLSDLLRNK RFRSRLPQMM EVYGPRNVEI VQRLLDDPRF APTHGGLPFP
     VWPLLKKSLT FVPKAKLELM RTLAFPDAAR TRAFRATEQL RYQAQAPEFA NSEQRLRFAE
     EVQRDFMTAS DVIWPLFVGI LVGQLPKSLL KGIASGPEVD VVLGGLPHNV TTEMDLALWR
     LTTRLGDDER ALLSSTPPAE LASRYRAGTL PDIGLEDFLA RYGHRAPAEV DVGMPRWAED
     PTQIFDTLAA YLKITDPEQA PDRRFQQAAA RAEAAIDELY ERARRRRPIR ARLARFCMRR
     ARKLTGLREL GKFAWLHSLR TVREQLLLIG EDLTRQGRLE RAGDVMFLDL DEIRAAIRGT
     DQRTPAAERK SFYDREVRRR SVPIAVLSDG TDLEAAAPSE PAADGAMTGL GASPGKVTGP
     ARVVHDPANA RIEPGEILVA TTTDPGWTPL FMTAAGLVTE TGSPMAHGPT VAREYGIPAV
     ICVRDATTAI TTGQVITVDA AAGTVTPE
//
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