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Database: UniProt
Entry: V6L0C1_9ACTN
LinkDB: V6L0C1_9ACTN
Original site: V6L0C1_9ACTN 
ID   V6L0C1_9ACTN            Unreviewed;       693 AA.
AC   V6L0C1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Pyruvate phosphate dikinase AMP/ATP-binding domain-containing protein {ECO:0000259|Pfam:PF01326};
GN   ORFNames=N566_11655 {ECO:0000313|EMBL:EST37673.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST37673.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST37673.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST37673.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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:EST37673.1}.
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DR   EMBL; AWQV01000376; EST37673.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6L0C1; -.
DR   STRING; 1380770.N566_11655; -.
DR   PATRIC; fig|1380770.3.peg.2027; -.
DR   HOGENOM; CLU_028596_0_0_11; -.
DR   Proteomes; UP000017915; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; 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   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017915}.
FT   DOMAIN          420..691
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  74882 MW;  1274760E6F50062C CRC64;
     MSTHDITHTT HGTDRSAPAG PARTVPVQGG PSGEHRHGAV LGGLLTLPLF EQLCGVLGGH
     PYVKVVVDRQ EGVWHVLDSS VHSFHVNYIA IEILGMTLDE LDADLDGFNH SVYHDPDRRF
     LLGVLSLHTD TAGPQSRPAQ PFMVLETTEA DTMGAALLTE FYTEVRGHLD ESLALAVKPA
     NHGQENAVAA VPETDLPRAQ GHELFSAAPF VPLTLGTATG RLRRFATEDD YRAARATLTW
     YDIVAMPVVP DDIPRLAGLL NAEPTTPLSH TNMLAAGWGV PNAIVRGVLD RIDDEKLDGA
     WVTYEVTTGG ARLETAEEPD DLAEPAWHTQ RIRLDAPSRD DLPIVPLASL RAKDRHAYGT
     KAANLGELHH VLRNGSARLT GYYAVPRPPR ADLLGHLAGR LGARTEGDEL AEAADDFLAR
     HVKAPEGVAV PFSLQQRFLD SSPAIQQSIG KLKMALELGA MDAVDAVCVQ LQHLVRTTPV
     PDDMARTLDG HLVRHLAGAS RFAVRSSSNA EDLPGFSAAG IYESHTQVAD LPDALDAIRQ
     VWASLLSPRS VRLRHEAGIS LDDTYMGVIV QRYEPSPLGG VMVTCNPTNR ADFRNVYLNC
     AHGSTAAVVD GSTLPMQYLY NTVEGGGRTL SLGAAERDLD AGTREQLARL ALAGRLLQSH
     YATDYTFAAP LDVEWLLTAE GVLHILQLRP YNA
//
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