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Database: UniProt
Entry: A0A101WN32_9FIRM
LinkDB: A0A101WN32_9FIRM
Original site: A0A101WN32_9FIRM 
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
//
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