ID Q8DQ39_STRR6 Unreviewed; 143 AA.
AC Q8DQ39;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 Name=lguL {ECO:0000313|EMBL:AAK99668.1};
GN OrderedLocusNames=spr0864 {ECO:0000313|EMBL:AAK99668.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99668.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK99668.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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DR EMBL; AE007317; AAK99668.1; -; Genomic_DNA.
DR PIR; H97979; H97979.
DR RefSeq; NP_358458.1; NC_003098.1.
DR AlphaFoldDB; Q8DQ39; -.
DR STRING; 171101.spr0864; -.
DR KEGG; spr:spr0864; -.
DR PATRIC; fig|171101.6.peg.952; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_4_9; -.
DR Proteomes; UP000000586; Chromosome.
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:AAK99668.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000586}.
FT DOMAIN 21..142
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 143 AA; 16513 MW; A8C03A4060FFAAE8 CRC64;
MRLEQDCPVF LKIKEKDMAS KMLHTCLRVE NLEKSIAFYQ DAFGFKELRR RDFPDHAFTI
VYLGLEGDDY ELELTYNYDH GPYVVGDGFA HIALSTPDLE ALHQEHSAKG YEVTEPNGLP
GTTPNYYFVK DPDGYKVEVI REK
//
