ID E1X4M5_HALMS Unreviewed; 891 AA.
AC E1X4M5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Phosphoenolpyruvate-utilizing enzyme {ECO:0000313|EMBL:CBW25455.1};
GN OrderedLocusNames=BMS_0544 {ECO:0000313|EMBL:CBW25455.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW25455.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
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DR EMBL; FQ312005; CBW25455.1; -; Genomic_DNA.
DR RefSeq; WP_014243242.1; NC_016620.1.
DR AlphaFoldDB; E1X4M5; -.
DR STRING; 862908.BMS_0544; -.
DR KEGG; bmx:BMS_0544; -.
DR PATRIC; fig|862908.3.peg.521; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_7; -.
DR Proteomes; UP000008963; Chromosome.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008963}.
FT DOMAIN 16..312
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 816..885
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 627..654
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 891 AA; 102281 MW; F367C5B3A6342616 CRC64;
MLLINKDTTE SFAKKQAGGK GYNLYLLARK GVNVPNFSVI PAYLFENFVE RNGLREAINE
ALEKASFKEA AKQIEEIILK GVFTANEKET IELLIKSFSS THFSVRSSAG DEDGGEHSYA
GQLSSYLYIS SLSKCLESIK KCWASAFSER CLVYRKENSI NLDRILVSVV IQEMIDPEIS
GVVFTCNPVT NNTEEIMINS VYGVGEGLVS GLLEGDTFIV SKIDAKVTSR EIVEKEKALK
GDFENERIIE VAIDKDKAEF ESLNEAQITQ LCSEATKIED MYQCAQDIEW AIYDDKIYIL
QTRPVTTLAA TSKGILNLWD NSNIVESYGG ITKPLTYGFA RYVYNQVYIQ FCEVLMVPQN
HIKEMNFFLK NMLGLFYGRV YYNLFNWYKL TSILPGYKFN RQFMETMMGT SESLGDEIAE
RIKPPKFHHS FGSRVRKFLT GFKFFYFHLN IQNIVDKFLI DFHKIYDVYR KKDYYSMSAD
QIYDEYMGLE KDILWKWHAP IINDFLCMVH FGVYKKLTEK WLDHLGQNFH NDLLAGNGNL
ESAEPTKQLI RLSGVVVKTN GLRDFIFANE NEFLLEALNQ SEYQEFYEMV KTYLDKYGFR
CMSEMKLEQK DMHLEPKLFF IFLKNIINSG QTNLEEFEKR EKEIRENAEK LLSENISGFK
GVIYSWSLKH ARKAVMNREN TRFCRTRIYG VVRSMFYAMG ENFAKSGIIA KDEDIFFLDL
EELKGAFEGT NSIQNLKEVI KTRKAQYELY EDSEPDSRFM TRGPVYWKNN HFPPPVVVDQ
NIELKENEML GLGCCPGIVE GVVKVILSPE DNLELNGEIL VTHRTDPGWI PLYPSASALL
VERGGLLSHS AIVAREMGLP TIVSVKGLTK RLETGMRIRI NGESGLIEIL E
//
