ID D2EP55_9STRE Unreviewed; 280 AA.
AC D2EP55;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glyoxal reductase {ECO:0000313|EMBL:EFA24869.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EFA24869.1};
DE EC=1.1.1.283 {ECO:0000313|EMBL:EFA24869.1};
GN Name=yvgN {ECO:0000313|EMBL:EFA24869.1};
GN ORFNames=HMPREF0850_00743 {ECO:0000313|EMBL:EFA24869.1};
OS Streptococcus sp. M143.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563037 {ECO:0000313|EMBL:EFA24869.1, ECO:0000313|Proteomes:UP000002766};
RN [1] {ECO:0000313|EMBL:EFA24869.1, ECO:0000313|Proteomes:UP000002766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M143 {ECO:0000313|EMBL:EFA24869.1,
RC ECO:0000313|Proteomes:UP000002766};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. strain M143.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG730097; EFA24869.1; -; Genomic_DNA.
DR RefSeq; WP_000844576.1; NZ_GG730097.1.
DR AlphaFoldDB; D2EP55; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_9; -.
DR OrthoDB; 9804790at2; -.
DR Proteomes; UP000002766; Unassembled WGS sequence.
DR GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd19071; AKR_AKR1-5-like; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EFA24869.1}.
FT DOMAIN 15..265
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 74
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 280 AA; 31634 MW; 4DD83A9BCA1CC816 CRC64;
MKSYTLNNGV SIPVLGFGTW KAENGEVAYQ AVLEALKAGY RHIDTAAIYQ NEESVGRAIR
DSGIPRQEIF VTTKLWNTNH SYEEARQAFE ESMEKLGLDY LDLYLIHWPN PKPLRENNEW
KTRNAEVWRA MEDLYKEGKI RAIGVSNFLP HHLDALLETA RVIPAVNQVR LAPGVYQEEV
VAYCREKGIL LEAWGPFGQG ELFDKKEVQE IADKHGKSVA QIALAWSLAE GFLPLPKSVT
ASRIQSNLDC FGIELSKEER EVLKTISVIS GAPRVDEMDF
//
