ID R6L204_9FIRM Unreviewed; 439 AA.
AC R6L204;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=BN564_01988 {ECO:0000313|EMBL:CDB68352.1};
OS Eubacterium sp. CAG:252.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262887 {ECO:0000313|EMBL:CDB68352.1, ECO:0000313|Proteomes:UP000017970};
RN [1] {ECO:0000313|EMBL:CDB68352.1, ECO:0000313|Proteomes:UP000017970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:252 {ECO:0000313|Proteomes:UP000017970};
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 -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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:CDB68352.1}.
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DR EMBL; CBEA010000099; CDB68352.1; -; Genomic_DNA.
DR AlphaFoldDB; R6L204; -.
DR Proteomes; UP000017970; Unassembled WGS sequence.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02320; PEP_mutase; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 19..109
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 439 AA; 49750 MW; 143CCB443A6A95F3 CRC64;
MNKGDSKIMK TVYTCFCTDV IHEGHLNIIE QAHKYGRVVV GALSDEALIR YNRFPTISFD
ERIKMYQELE GVDEVIVQNT IMYDDVIKKL KPDYVVHGDN WREGAESVIR ENVLSLLSEY
GGELIEVPYT YNEKVRKIDS TLKEKLAMPE YRRKRLKQLI KMCPVVKTIE AHSGLTGLIA
EKTVVEENGR LDQFDAMWVS SLCDSTAKGK PDIELVDMSS RLRTIDDIME VTTKPIILDG
DTGGLTEHFV YNVRTLERMG VSAIIIEDKK GLKKNSLFGN EVEQTQDSIE DFSAKIAAGK
KAQLTDDFMI IARIESLILE KGMEDALTRA FAFVKAGADG IMIHSRKKDP TEILEFCDEF
RKKDANTPIV VVPSSYNVIT EDELAAHGVN IVIYANQLTR SAFPAMRQTA EDILRYHRAK
EVDDRLMPIK DIITLIDEL
//
