ID E4L135_9FIRM Unreviewed; 126 AA.
AC E4L135;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Aldoketomutase {ECO:0000256|ARBA:ARBA00030892};
DE AltName: Full=Ketone-aldehyde mutase {ECO:0000256|ARBA:ARBA00030291};
DE AltName: Full=Methylglyoxalase {ECO:0000256|ARBA:ARBA00032460};
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase {ECO:0000256|ARBA:ARBA00033298};
GN ORFNames=HMPREF9286_0389 {ECO:0000313|EMBL:EFR32174.1};
OS Peptoniphilus harei ACS-146-V-Sch2b.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR32174.1, ECO:0000313|Proteomes:UP000003705};
RN [1] {ECO:0000313|EMBL:EFR32174.1, ECO:0000313|Proteomes:UP000003705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR32174.1,
RC ECO:0000313|Proteomes:UP000003705};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFR32174.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AENP01000032; EFR32174.1; -; Genomic_DNA.
DR RefSeq; WP_005958119.1; NZ_AENP01000032.1.
DR AlphaFoldDB; E4L135; -.
DR eggNOG; COG0346; Bacteria.
DR Proteomes; UP000003705; Unassembled WGS sequence.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR PANTHER; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR46036:SF5; LACTOYLGLUTATHIONE LYASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS51819; VOC; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:EFR32174.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003705}.
FT DOMAIN 2..123
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 126 AA; 14865 MW; 010EC54873E603E6 CRC64;
MKFLHTMIRV KDLERSEKFY KEALGFVESR RKDFPEDEFT LLYLKLEDSP FELELTYNYD
GRDYTIGDGY GHIAISHPDI RSFREELKNK GCDVTELKAL SDKSDSYFFV KDPDGYKIEV
IGEKNK
//