ID A0A258H2Y6_9PROT Unreviewed; 878 AA.
AC A0A258H2Y6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B7Y90_01790 {ECO:0000313|EMBL:OYX51380.1};
OS Alphaproteobacteria bacterium 32-64-14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1970492 {ECO:0000313|EMBL:OYX51380.1, ECO:0000313|Proteomes:UP000215897};
RN [1] {ECO:0000313|EMBL:OYX51380.1, ECO:0000313|Proteomes:UP000215897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-64-14 {ECO:0000313|EMBL:OYX51380.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OYX51380.1}.
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DR EMBL; NCEM01000003; OYX51380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258H2Y6; -.
DR Proteomes; UP000215897; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
FT DOMAIN 58..197
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 203..253
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 792..863
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 265..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 93873 MW; E0FA0E9621431458 CRC64;
MSDHARILFG ADAVVPEAGG KGAALAKLAA MFPVPAFFVI GAEAFDQAGL KAEAREEVER
GLQRLGGAGR FAVRSSGLEE DGASSAHAGQ FATELNVAAA DVEAAAHRVW LSGFTESLAA
YRVAHGLSGD PQPPAVIVQV MVAARAAGVA FSADPVSSDR SVVVISAIVG LADRLVGGEE
DGDSYRIGAD GGTLEAQLVG EVAVLSEAER SEVAAMARRA ADHFGLPQDI EWAFDHAGLK
MLQSRPITTL GGALEVESFS AKRVGARAEN PGSAGAGTSG SSAHETTGIP GMRASRLPEN
DSASEETIWD NSNIVESYPG VTSPLTFSFA RYVYAHVYQA FSRLMGVPGA DVEEHRAVFE
NMLGRVDGRV YYNLLNWYRA LALFPGFKAN RKFMEGMMGV SEALPQEMAD RIAPPSDSEW
EKFIDNLKFG RVGLGLVWHE IRIKGTIAKF YARLNAALVR PDGEIDAMQA TSLAAEYRLL
ERQLLAKWDA PLVNDFLCMI AFGLAQKTME REGGDEGRAF LSNMLIGQGD IVSAEPARMI
REMGAMVRGQ PELVARLAKG DRGAVDTDPA LRAAFDRYIA KFGDRCTQEL KLESRTLHED
PAQVLMAISA AAATRGAETV KEAEGDLHDI VPEFGKRVVA RWMLDWAKAR VRDRENLRFE
RTRLFGRVRR ICLALGARLS EAGVLNDRRD VFYLTVEELL GAVEGAAITG DLKALVRLRQ
AEWDAQLKRP DPPERFSARG AHVVGVAELS AQAPTNVTGP DAGGETRKGL ACCKGVVTAK
VRVIDDPRVE ALSPGEILVA RHTDPGWIAV FANAAGVIAE RGSLLSHSAI VAREMGVPCV
VSLKGVTQWL RTGDVVRLDG GAGTVERIGG ADKAGTAA
//
