ID A0A1G2M1D1_9BACT Unreviewed; 485 AA.
AC A0A1G2M1D1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=PEP-utilising enzyme mobile domain-containing protein {ECO:0000259|Pfam:PF00391};
GN ORFNames=A2664_03730 {ECO:0000313|EMBL:OHA17700.1};
OS Candidatus Taylorbacteria bacterium RIFCSPHIGHO2_01_FULL_46_22b.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802301 {ECO:0000313|EMBL:OHA17700.1, ECO:0000313|Proteomes:UP000178873};
RN [1] {ECO:0000313|EMBL:OHA17700.1, ECO:0000313|Proteomes:UP000178873}
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:OHA17700.1}.
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DR EMBL; MHRF01000013; OHA17700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2M1D1; -.
DR STRING; 1802301.A2664_03730; -.
DR Proteomes; UP000178873; 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 407..479
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 485 AA; 54928 MW; 0BBAEA22964B116D CRC64;
MKKIDLESIQ ESDLTYFGER AEPPFGSSAI ISGMQNRELS RSLLGLETIV RWLQVNHYFY
QFAGDLLEIE AEVKNKFDVS NNQYINSLIE QCLQAGDKLR EVSLLFRKYV GDKSADKKVL
ADAILVYSRA LSHYTVFYQI TFFERPLVEF AEELVKKYTA NKEEAQKLYD TISVADRLTT
AEYEQDDFLR LAGIREEELP IVAENHAQKY GWLGVRYFIG DAWTKETVLK RLEGINKTKA
LHELEIRLAH RKEREQKIEK AISSFSVQDK HVVDIIRKVV YLRTQRGDFV HESAAIVRPV
LDKIAQLLNI SYEGLICLSA DEVSTALKGE FDYVSHVKNR LENFLIYHVQ GDEYRILEGA
EVVSFVQSHP FLDMTKDAVT EFSGKTGYAG CARGTVKIIK TGKDVEKFER GDILVTTMTT
SNLLPALEKA SAFVTDEGGI TCHAAIMARE MRKPCVVGTK IATHVLKDGD IVEVNADTGV
VKIVK
//
