ID A0A0Q8Q497_9ACTN Unreviewed; 502 AA.
AC A0A0Q8Q497;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate phosphate dikinase {ECO:0000313|EMBL:KRB80429.1};
GN ORFNames=ASE01_02860 {ECO:0000313|EMBL:KRB80429.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB80429.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB80429.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB80429.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB80429.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB80429.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB80429.1}.
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DR EMBL; LMIA01000001; KRB80429.1; -; Genomic_DNA.
DR RefSeq; WP_056748470.1; NZ_LMIA01000001.1.
DR AlphaFoldDB; A0A0Q8Q497; -.
DR STRING; 1736488.ASE01_02860; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000050886; 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:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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 Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 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 InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 3.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRB80429.1};
KW Pyruvate {ECO:0000313|EMBL:KRB80429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW Transferase {ECO:0000313|EMBL:KRB80429.1}.
FT DOMAIN 22..59
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 62..242
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 259..306
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 378..447
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 502 AA; 51818 MW; 0EC26994EB26ECDC CRC64;
MSTVVSTGSV VALAGDGGHS REEIGGKAWS IQQMLGLGIP VPPAFVVTTD VCRAYHRAGG
TLPDEIWQEV VAAVAGIEQA VDRCFGGERP LLVSVRSGAS TSMPGMMDTV LNLGINAASQ
ERLAQETGST AYAADTRVRF EEQFAKVVGA PAPEDPWEQL YLAVCAVLES WFSKRAIAYR
AARGIPDDGG TAVTVQAMVF GNLDDDSGTG VLFSRDPLTG GGSVYGEWLA RGQGEDVVSG
RADALPLDTL AQAQPQVHAE LMEATRTLER EGRDVMDIEF TVQSGTLWLL QSRPAKRAPE
AAVRSAIHLA EAGVIDRDEA IARIRPDDVR ALLRPRLAAA DVAASPAVAT GKPACPGIAV
GVVVTDADEA EDRADDGESV VLVRPTTDPD DVAGMAASVA VVTEIGGSTS HAAVVCRELG
LPCVVGTGTD TLMALAGQVV TVDGGSGTVH LGALAVEPAA TADDPALATL REWLGIEDSD
PASVVARLAA GAPGTSTSEE GR
//
