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Database: UniProt
Entry: A0A0T1WDH1_9MYCO
LinkDB: A0A0T1WDH1_9MYCO
Original site: A0A0T1WDH1_9MYCO 
ID   A0A0T1WDH1_9MYCO        Unreviewed;       493 AA.
AC   A0A0T1WDH1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASD37_13490 {ECO:0000313|EMBL:KQY07096.1};
OS   Mycobacterium sp. Root135.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY07096.1, ECO:0000313|Proteomes:UP000051127};
RN   [1] {ECO:0000313|EMBL:KQY07096.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY07096.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY07096.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY07096.1,
RC   ECO:0000313|Proteomes:UP000051127};
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:KQY07096.1}.
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DR   EMBL; LMEZ01000005; KQY07096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T1WDH1; -.
DR   STRING; 1736457.ASD37_13490; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000051127; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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; IPR018274; PEP_util_AS.
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; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT   DOMAIN          71..244
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          376..445
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   493 AA;  50746 MW;  EB2CD242312F0B37 CRC64;
     MSGHAMTIGA GSRHAVPLDG ELTGAARLAV GGKGRAVAAM AALGLAVPPA FCVTSDWSDD
     DPSALVDRLW QDVLDGLKVL EERTGRTFGA GPRPLLLSVR SSGDTSMPGM LETVLNVGLD
     DAVVEALGKE YSVGFAEDTR ERFRRGYRRA VGVEAPGQPL AQLRGAVEAV ASSWSSSRVD
     AYRAHRGLER GGIAILLQAM VFGNLDAQSG TGVLFTRDPA TGASTPFGEW LPAAQGDDVV
     SGTSDCEPLS AMRDRLSAAY DELVEAGARL ERLGADVQDV EFTVEAGKLW LLQSRVAQRS
     PRAALRLALT FRDEGLVDDA EVIERVTPEQ LATILAVRSA PSGPPLATGA AACPGIASGL
     VCTTSDDAIA AADAGRDVIL VRPTTSPDDV AGIMAANGVV TEVGGASSHA AIVARELGIP
     AVVGCGVGLT ASLAGLTVTV DGDAGEVRAG ESAASESVLS PELSRFADIV RAAVPDVVGD
     LQAMHRVARS ARR
//
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