ID A0A101WN32_9FIRM Unreviewed; 877 AA.
AC A0A101WN32;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=APF77_00415 {ECO:0000313|EMBL:KUO76075.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO76075.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO76075.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO76075.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO76075.1}.
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DR EMBL; LOES01000045; KUO76075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WN32; -.
DR STRING; 1734399.APF77_00415; -.
DR Proteomes; UP000057710; 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; 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;
FT DOMAIN 17..310
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 803..872
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 877 AA; 98168 MW; 2B80578EB984E0DD CRC64;
MELIYRFDTN EASELAKVGG KANSLILMTR HGLPVPTGFV LSVEFFKPWY DQLKETPEWQ
RVVNSSPQEL KMHTNALKKA CESLRLDEVR RKSLTEALDS IKTGSRELLF AVRSSSPEED
LEGASFAGGY ETTLGVKKEK AEAALLHSFV SSLDERVFVY KKEHGFRMDD PKIAVIVQVQ
IPSDTAGVAF SLNPVNNCYD EAVINANFGL GETVVSGSVS PDTFIVDKVS GKILEKKAGR
KETSIWLAAD GGTYEKPSPS QQSLSLSDDN INTLMNMLIT VENYYKKPVD IEWAFAEGRL
YLLQARPITA YIPLPEELQT VPGRQKLLYL DQTLAKQGIH EPLSVMGTDL LSFFGEKIEK
AMTGRSVPDV ADGISGSLEG RMYLNISNNI KLYGKKKLIN TYRSIDKPSA EIIEHMDAEE
YVPKALPLKL RGVIWGTLQN SLGMMVNVFK ALKDPEGYEK KLIEQAELFI ADMRKELDSG
QSVMKFANSV TDRFVSFFVF SLPLLVVIAV AKAGIEKIFK DSGEEIRSKV TYLEKAMPNN
VTTEMGLSMY RLSRFEEISK CRSFEEFKEK LESKAFSGDF MNPWGSFIER YGFRCPRELD
IATPRYYEQL EMLYGQLKGM AGNTDAEHNP QAIFDSARAE REKEYKELLR EAGSKGKSKA
KKFTKYYKML VRFLGYREAP KYYWIMTVDV LRKKVLEAAE ALKLSGRLEH VDQVFDLKIE
DLERAITDQS VDIGAMISRN TAFLKKLANI HEFPRVIDSR GRILYPPKKK AVTGELAGEP
ISPGIIRGKV KVLRSPEEKP VLPGEILVAR ATDPGWTPLF INAAGVILEV GGVLQHGALV
AREYGKPCVS GIEDAVSILK DGQMVEMDGL NGIVRLL
//