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
//