ID   A8X8K2_CAEBR            Unreviewed;      1241 AA.
AC   A8X8K2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Protein CBG09648 {ECO:0000313|EMBL:CAP28963.2};
GN   ORFNames=CBG09648 {ECO:0000313|EMBL:CAP28963.2,
GN   ECO:0000313|WormBase:CBG09648}, CBG_09648
GN   {ECO:0000313|EMBL:CAP28963.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP28963.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP28963.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP28963.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; HE600998; CAP28963.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X8K2; -.
DR   STRING; 6238.A8X8K2; -.
DR   WormBase; CBG09648; CBP42564; WBGene00031206; -.
DR   eggNOG; ENOG502QS3J; Eukaryota.
DR   HOGENOM; CLU_005950_0_0_1; -.
DR   InParanoid; A8X8K2; -.
DR   OMA; WRSVKSH; -.
DR   OrthoDB; 3092388at2759; -.
DR   Proteomes; UP000008549; 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; 2.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549}.
FT   DOMAIN          390..611
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          1161..1230
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   1241 AA;  140932 MW;  04D863FD35B43C5F CRC64;
     MLILLLLIFI SAPLCRYILY PVVYAFLKWR RPVRKFTAPT AKIRDILNPD KDEWNMEEIK
     NEEIITISGS GEDDSFVYIQ IITKNGIHSS HIRIFENGTL YSGSFDAYFA ENRTIICGPL
     IIELRNPFRK WRINFRGYLK DNDGNSHFII LSGWWRCVTN ARFFYSNAPL KSFTDVYHEK
     PLELAENLKT IEKYRTGNVF HQMGEYHAEI KIGNGEVVEH RYRGLRHRNP LNLETTSTQF
     HTYLSDGNAI SHRVNSLEHQ KLVSHAIIFR ADHSVRAVTL HNSHSLESDN MMPVRFNYSS
     GKFLPFEMRK GQKLSHFNYI REDRKVVDVT ALKVNSAIFT GIGFVVRIRE ALHTTPAKTL
     DCFPEYHATD SEKVRQVLPF GHRACQDKLL TGGKGANLAR LQAITNDFHV PPGIVVTTAA
     FNEHVRMNRN IAEAIKLLDQ NDQSANYYEE TGKRIGELLI ESEVSEELHN KIREWLPFSE
     YYAVRSSAVG EDGADLSSAG QLESYLDVFS HEISDKLKLC WASNFRREVL NYRKNYGQQL
     NPSMAVVIQE MNRNGVAGVM FTANPVKLDC GEIVINALKG SGEQIVSGVT TPDEIHVNRI
     NKSVVINKIG TECCLNDFQI EKLSRVGEYL ERIFGKPQDI EFVVRGDQVN IVQSRDITGL
     DKETSFEMYT EYNSPSIHDK EILTNANVGE VLPAPVNAME AHNLTGMFDK VICVSLDQCM
     TTQEINDVVP AHTTIGFSVA HRKIFFNLGE VVLRIWEMVE KDRITDIVIA GETLFSPEMF
     RQAAHQYGSV PSFFPLKRMY RMIKLIYFTS NSVKAKIAEI DKEAKLLVPT EDMSVEEVFK
     KYEELEKLWC DAIRCHTDLS MFSSFTYVLC GMLIRGSDTG PLSNDNISDF ANVFSNNSRG
     DVVSADVPNS LKKLAKTIRE DGLVKEFCDA EGNDSLKILE NGRRSSQELQ RFFDLHGHRG
     PKELYLDAAT WEEDTDLLVH TIKSMLSFPE ASDKTIENED DIIDKLKCKP TGIRRRFLKY
     FIGQTHRGVA FRETAKNHLV STTNSVRKTC RMIGKKLYQK GYLPDPNLWM HFSIDELKEL
     NETRSAKLIS RAVRRKQIAS KFEGLQFPLV AHGYMSPIKV EIAETDASVG LTLRGTTVCE
     GKVRANARVA KTLEEAKETI PGEILITRYT DICWSPFFPM ISGIVTEIGG LLSHGAVVAR
     EYGLPSLIAV TNATQHFKTG DFVELDSING TIIRLDQNHN D
//