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
//