ID A0A1Y4NCB9_9FIRM Unreviewed; 442 AA.
AC A0A1Y4NCB9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=B5F08_06920 {ECO:0000313|EMBL:OUP78486.1};
OS Anaeromassilibacillus sp. An172.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965570 {ECO:0000313|EMBL:OUP78486.1, ECO:0000313|Proteomes:UP000195869};
RN [1] {ECO:0000313|Proteomes:UP000195869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An172 {ECO:0000313|Proteomes:UP000195869};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP78486.1}.
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DR EMBL; NFKS01000011; OUP78486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NCB9; -.
DR Proteomes; UP000195869; 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; TIGR00125; cyt_tran_rel; 1.
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};
KW Pyruvate {ECO:0000313|EMBL:OUP78486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195869}.
FT DOMAIN 22..107
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 442 AA; 50156 MW; 7B5C3A921FECBC22 CRC64;
MYAERRAVMS ENKVVYTCFS TDVIHKGHLN IVNKAKELGK VIIGVMSDEA AVKYDRFPTI
SFEERLNMIK NIDGVSEAVP QETVSYKDNL LKYKPDYVVH GDEWKYNYMA PIRQEVIDVI
SQWGGRLVEV PYTRDDEVRK IDRQTMEKLS MSEFRRGRLR KLLKLRPVVK AIEVHSGLTG
LIAEKTVVEN NGEVDQFDAM WISSLCDSTA KGKPDIELVD MSSRIRTIED VLDVTTKPII
FDGDTGGKTE HFVYNVRTLE RIGVSAVIIE DKVGLKKNSL FGTEVEQTQD TIENFCNKIK
AGKNALLTDD FMIIARIESL ILEKGMEDAL ERAKAFVGAG ADGIMIHSRR KEPDEIFEFV
DKFREFDKET PIVVVPTSFN TVTEEEFAKH GVNIVIYANQ LTRTAFPAMK NAAELILKNH
RAKEADDICM PFKDIITLID SI
//
