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Database: UniProt
Entry: R5JEI0_9FIRM
LinkDB: R5JEI0_9FIRM
Original site: R5JEI0_9FIRM 
ID   R5JEI0_9FIRM            Unreviewed;       785 AA.
AC   R5JEI0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate binding domain protein {ECO:0000313|EMBL:CCY52983.1};
GN   ORFNames=BN781_01387 {ECO:0000313|EMBL:CCY52983.1};
OS   Coprococcus sp. CAG:782.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=1262863 {ECO:0000313|EMBL:CCY52983.1, ECO:0000313|Proteomes:UP000018002};
RN   [1] {ECO:0000313|EMBL:CCY52983.1, ECO:0000313|Proteomes:UP000018002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:782 {ECO:0000313|Proteomes:UP000018002};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCY52983.1}.
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DR   EMBL; CAYJ010000011; CCY52983.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5JEI0; -.
DR   STRING; 1262863.BN781_01387; -.
DR   Proteomes; UP000018002; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
KW   Kinase {ECO:0000313|EMBL:CCY52983.1};
KW   Pyruvate {ECO:0000313|EMBL:CCY52983.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018002};
KW   Transferase {ECO:0000313|EMBL:CCY52983.1}.
FT   DOMAIN          34..126
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          709..779
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   785 AA;  89255 MW;  2113CFF0D4F09137 CRC64;
     MFYTKADMLR FLSDKVTLSR IEHIMTLSGN EYYKDMDKAA GEVCKEFAGG LVVVRSSSSM
     EDGEKNSNAG HFDSVLNVDS SDPDSVKSAI ERVFASYDSD VNDEEVLIQN QVKDAVISGV
     LFTRDIKGNR PYYVINYDDK STDTVTAGLG GRILYVWHEC ESTRLKAPFD SLLTAAREIE
     DILPDYPLDI EWAVDSKGEV IIFQTRPFAA AINGEPGKLS DDEWKQAITG AVKSYESVCN
     ELGEPAGTML SDMAFWNPAE MIGTNPHPLD YSLYREIITK HAFNQGLNYI GYREVDGELM
     YKIGNKPYIS LKQSFLCLTP DDLENRLVRK LMKYYNKKLL EDRTAHDKIE FEIVFSNYDF
     TTEEKLAVLR DEGFTEEEID DIRDALFNLT NNAICNFKLN RMKDLRALNG LRVHRENTRN
     NWIMSERTCH TSIGYFVELI ESIKQYGTPK FARQARLAFI SKALCRSFVS AGYFTSGEID
     DFMMSIYTVA AEYDADFQDL VDGRITRVEF DERYGHLRSG TYDITCDTYE KREFDMNKGS
     ANARKQRQRL ETLKHNPLNV LTIIDALDKL GFYVDATEFV EFLKESMEER EYFKFEFTKS
     LSLALDILAD LGEYLGLTRE EMSYLTFNDI VKCANIPEED IAASFKADID KNRSEYRTYS
     ELVLPDVIAD KTELDVVHIV QARPNFITSD VVTGEVVCLE DDNTQDVAGK IVVIQKADPG
     FDWIFAKGIK GFITKYGGVA SHMAIRCAEF NIPAAIGCGD VIYNRVCSQD RIILDCRKGK
     IEMVD
//
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