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Database: UniProt
Entry: X1PYZ2_9ZZZZ
LinkDB: X1PYZ2_9ZZZZ
Original site: X1PYZ2_9ZZZZ 
ID   X1PYZ2_9ZZZZ            Unreviewed;       389 AA.
AC   X1PYZ2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Pyruvate, water dikinase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=S12H4_01275 {ECO:0000313|EMBL:GAI61482.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAI61482.1};
RN   [1] {ECO:0000313|EMBL:GAI61482.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAI61482.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:GAI61482.1}.
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DR   EMBL; BARW01000242; GAI61482.1; -; Genomic_DNA.
DR   AlphaFoldDB; X1PYZ2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..74
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          96..382
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAI61482.1"
SQ   SEQUENCE   389 AA;  43240 MW;  EF5965B387F381C4 CRC64;
     DKVLDGDILV AEMTTPDFVP AMKRAAAIVT DRGGRTAHAA IVSRELGIPC IVGTGQATKM
     LTNGQIISVD GARGKVYEGR VAVRERADDT YKENIKTKTR VYVNLAQPEL VERVAARNVD
     GVGLLRAEFM VAQIGEHPSY MISQNRGNEF VDKLAEGIGA FAKAFSPRPV VYRTNDFKTN
     EYRELTGGQE YEEAEENPML GYRGASRYIA DIDVFKLELE AIKRVRQDYK NLWVMIPFVR
     TVDELARTEE IMESEGLKRS DDFKLWMMVE VPSNIFLMEK FLAVGIDGIS IGSNDLTQLI
     LGIDRDSEKL AETFDERNEA VLIALERAIK VSKSMGVTSS ICGQAPSVYP ELTEKLVEWG
     ITSVSVSPDM IGTTREIIAK AEEKLKLND
//
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