ID G2KLW3_MICAA Unreviewed; 777 AA.
AC G2KLW3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Pyruvate phosphate dikinase, PEP/pyruvate binding domain protein {ECO:0000313|EMBL:AEP09342.1};
GN OrderedLocusNames=MICA_1012 {ECO:0000313|EMBL:AEP09342.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09342.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP09342.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09342.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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DR EMBL; CP002382; AEP09342.1; -; Genomic_DNA.
DR RefSeq; WP_014102565.1; NC_016026.1.
DR AlphaFoldDB; G2KLW3; -.
DR STRING; 856793.MICA_1012; -.
DR KEGG; mai:MICA_1012; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_011659_0_0_5; -.
DR OrthoDB; 3590125at2; -.
DR Proteomes; UP000009286; Chromosome.
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; 1.
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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEP09342.1};
KW Pyruvate {ECO:0000313|EMBL:AEP09342.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Transferase {ECO:0000313|EMBL:AEP09342.1}.
FT DOMAIN 57..167
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 701..768
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 777 AA; 86554 MW; 9611AB6DD290FCA8 CRC64;
MKHSYATPVL STKSKTLESL SGRIATARIL PLHYFTVEDW RSGKAAVLKS IRGILGDVPY
IVRSSAVNED SATQSMAGQF ESILNVFNDS ELDEAVEKVI SSYGSDVNLQ DEILVQPMLD
DVRFSGVAFS HDPSTGAKYK VINFSIGSDT EAVTAGASET GCYVASDQAD NIVPYLRPIV
SVLDELSGIF SDRPLDVEFA VCGDDSTVYV LQVRPLIMKV DLYNSLEHKE LLARIAKKVR
SAQQPHPYLH GHSTVFGVMP DWNPAEIIGI RPRPLALTLY KNLVTDSIWA YQRHNYGYRN
LRSFPLLVHF AGQPYIDVRL SFNSFIPADI DGYLADQLVD YYINRLIQAP TLHDKVEFEI
VFSCYTLDLP ERLKVLDAAG FSDKERGMIA ESLRSLTNKI IDKDEGLWRV DAQKIEELVV
RREKILSSNL DHVSKIYWLL EDCKRYGTLP FAGLARAGFV AVQMLRSLVS VGVFSEDDYN
CFMNGLNTVS SQFSRDLSTL DKTSFLSRYG HLRPGTYDIL SKRYDESPDE YLGGTVHTGH
ANSNRKTFSL TLDQMKRVTD LLKEHGLSCD VMSLFDFIKS GVELREYSKF IFTRSLSDAI
LLFQSWGKQF GFSEDDLSYA DIGCVQDLYA SADDPREVLA RSIQKGRDDY AKTCRLWLPP
LITKPDDVFS FFMSESEPNF ITQSSVMGAV VGADDISKLS GAIVFISSAD PGYDWLFSYP
IAGLVTAYGG VNSHMAIRAN EMGIPAVIGA GEVLFKRWGA ANKIHIDCAG KSVKVIS
//
