ID A0A0N1N948_9ACTN Unreviewed; 717 AA.
AC A0A0N1N948;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:KPH98011.1};
GN ORFNames=OK074_0769 {ECO:0000313|EMBL:KPH98011.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPH98011.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPH98011.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPH98011.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPH98011.1}.
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DR EMBL; LJCV01000307; KPH98011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1N948; -.
DR PATRIC; fig|1592327.3.peg.8827; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000037991; 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; 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:KPH98011.1};
KW Pyruvate {ECO:0000313|EMBL:KPH98011.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000313|EMBL:KPH98011.1}.
FT DOMAIN 60..189
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 206..263
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 609..679
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 674..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 74913 MW; 6C04E1E1A0C51894 CRC64;
MGLQVTSLAV VPLDTKQAED PAVTGAKAAN LARSAVAGLP ALPGFVLVPT ERAPGAPGGE
AAIRTAWERL AAADGSPRAL VVRSSSAHED TEDSSMAGRF DSVLDVRGWE EFLAAVRKVL
DSARRVQLLH PPENAAPDDD GMAVLVQPML RAAVGGVMFT ADPVEGRTDR LLVSVVKGGP
DQLVDGSTQG VRYQLTRFAR LVRTEPAEPR GQRLLSHRRI TRLVALAKKT ERVFGGPQDM
EFGFDADGKL WLFQARPITA MAARPAPGAR LRGPGPVAET LPGVLQRLEE DLWVAPMSHG
LTLALDIAAA APRRVLRKLP LVVTIDGRVA ADLRLLGAVP SPHPVLDFIN PAPNARRAGA
AWRMGRLRSA LPLLAVDLMA DVDSALSDIP EPRQLLGGQL LDAVAWGREV LSALHAQESL
AGALLGPGSG ATGAGEALAQ LAEGRARGLD DEELLDRHPV LLALLPPTLG TRLPLPDNTG
WTALPRGVGA LPVREGLRLR LRWVQEMQAQ MVRELAGRLE AGEYEPGASR LWLLGWDELV
EATEGKGLPA DLAEREPRPD TGPLPAVFRV ADGRPVPAVL PGQRTSGDGQ GAGGGFGTGT
AWDGEGERPE QAVLVVRSLD PALAPLLSGL AGLVAETGSA LSHLAVLARE FHVATAVGVP
AAVDRFPNGT PLSVDGTTGA VTVEGTDEAD GAGPTDRADA ASTALITNGT NGQEPAA
//
