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Database: UniProt
Entry: M0PAQ2_9EURY
LinkDB: M0PAQ2_9EURY
Original site: M0PAQ2_9EURY 
ID   M0PAQ2_9EURY            Unreviewed;       892 AA.
AC   M0PAQ2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:EMA66933.1};
GN   ORFNames=C461_09252 {ECO:0000313|EMBL:EMA66933.1};
OS   Halorubrum aidingense JCM 13560.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA66933.1, ECO:0000313|Proteomes:UP000011575};
RN   [1] {ECO:0000313|EMBL:EMA66933.1, ECO:0000313|Proteomes:UP000011575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA66933.1,
RC   ECO:0000313|Proteomes:UP000011575};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA66933.1}.
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DR   EMBL; AOJI01000024; EMA66933.1; -; Genomic_DNA.
DR   RefSeq; WP_008000596.1; NZ_AOJI01000024.1.
DR   AlphaFoldDB; M0PAQ2; -.
DR   STRING; 1230454.C461_09252; -.
DR   PATRIC; fig|1230454.4.peg.1865; -.
DR   OrthoDB; 23397at2157; -.
DR   Proteomes; UP000011575; Unassembled WGS sequence.
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:EMA66933.1};
KW   Pyruvate {ECO:0000313|EMBL:EMA66933.1};
KW   Transferase {ECO:0000313|EMBL:EMA66933.1}.
FT   DOMAIN          23..316
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          811..881
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   892 AA;  95810 MW;  0C4496537888308A CRC64;
     MTQNPRSHYV RRFDSLGAAD LGVAGGKGAN LGVLVDAGVP VPSGFVVTTA AYRSIADDAE
     ISAAIERLGS HDPRDSGALT TTAAEIRALI RERPIGDPIE RAIAEALDVG ADTTYAVRSS
     ATAEDLPTAS FAGQHDTHLG VTADAVTDGV RDCMASLFTD RAVAYRARNG IAHTDVEMAV
     VVQRMVDADA AGVLFTADPE TGKRTVATVD ATYGLGDAVV AGEVSADHAR IARETGAVIE
     YDVGDKATER RLTRAGTTSV DTRTDRRETR VLTDAQLRTL VDIGERIEAL FGEPQDIEWA
     LVDGAFVILQ SRPITSLVSL PVPRPDDDRL HVYLSLGHGQ AMTDPMPPLA LDLWEAVYGD
     VMNGFTGRDR AWITRTEGRA YMDITPFLGF RRTREGIVKT IAAVNRSAAE GTERLLAERR
     EEFGIDVSLA TLPALLRTVA SVLPILARLF WQGIAPFVRG AAGIDEFVTE LNEWASAQAA
     DILATDDPAE LVETVFAGFS TEFVSDLSPK SMRVVIGPLA GTVLERVVSG ADAATVEAAA
     RGNEAEVGTR MTLALGDIAD VARETPAVER AILDGQPYEE VRAVDGSEAF VQAFDAFIDE
     FGHRAVGEFD PSRPRWRDDP SAPLGIVRGN LAGEDRGAHR SRLRERKREA QAAIDELQAS
     ADRGLLGPVR GPLVNHLLRT YRSHIHLRDE PKHAIAHLFA AWHEAIQRAG EHLVREDVLD
     DPDDVWFLRR SELRSLVDDP DGEVPDIAAR KRDHERHGRI DIPPLITSEG EIPRVERVDV
     DEHTLVGTGV SAGVVEGVAR IVDDPATTTL RSGEILVCPS SDPAWTPLFA TAGGLVTEVG
     GSLTHGALVA REYGLPAVVS VAGATEAITD GQRIRVNGDT GTVELLTKLD KR
//
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