ID A0A1F6SB61_9BACT Unreviewed; 451 AA.
AC A0A1F6SB61;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PEP-utilising enzyme mobile domain-containing protein {ECO:0000259|Pfam:PF00391};
GN ORFNames=A3G09_01035 {ECO:0000313|EMBL:OGI30147.1};
OS Candidatus Moranbacteria bacterium RIFCSPLOWO2_12_FULL_48_12.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1801643 {ECO:0000313|EMBL:OGI30147.1, ECO:0000313|Proteomes:UP000176289};
RN [1] {ECO:0000313|EMBL:OGI30147.1, ECO:0000313|Proteomes:UP000176289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI30147.1}.
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DR EMBL; MFSB01000040; OGI30147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6SB61; -.
DR STRING; 1801643.A3G09_01035; -.
DR Proteomes; UP000176289; Unassembled WGS sequence.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
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 371..443
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 451 AA; 51805 MW; C85C95582FB6937B CRC64;
MNIHDFEKRK WVVLGANCYP LYADSFAEPV SQGYYRIYGI PNEVLGIFSK DFFEWLYDDA
QLVALSEKLL PGLLNAPWNY YDEWQKNAKF FSTFHESVIE KDFTVLSHKE LGKLAKEYHR
IFWLQFAPSN IIEPLSYYFQ SRFKKMLTLK GVKENEIDQL MDHYGRSKYP NYVKECLVEY
RLAKNEDAIQ AVLKKYAYLA NDYLGPKILT KAYLDELLKQ ETHEPHVGAV SAVSPETQSL
LEVFQMVATI QDVRKAYSLM MVAGVHNFGI EYAKLLKLPD TLIWYALWKE IYAGDVDEKK
LEERRKQCII FWGKERIDIC EGEEAEELVR DTHKIVFGNV GELKEIKGIC ASPGKVSGRA
VIIMHPDEFL KVKKGDILFT MMTRPEFLPV MQLSAAFVTD EGGITSHAAI VAREMKKPCI
IATKIGTKVV KDGDMVEVDA NKGIVKIIEK V
//
