ID C2BH88_9FIRM Unreviewed; 127 AA.
AC C2BH88;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=gloA {ECO:0000313|EMBL:EEI85731.1};
GN ORFNames=HMPREF0072_1708 {ECO:0000313|EMBL:EEI85731.1};
OS Anaerococcus lactolyticus ATCC 51172.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI85731.1, ECO:0000313|Proteomes:UP000005984};
RN [1] {ECO:0000313|EMBL:EEI85731.1, ECO:0000313|Proteomes:UP000005984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI85731.1,
RC ECO:0000313|Proteomes:UP000005984};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2008) 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:EEI85731.1}.
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DR EMBL; ABYO01000247; EEI85731.1; -; Genomic_DNA.
DR RefSeq; WP_004828173.1; NZ_GG666046.1.
DR AlphaFoldDB; C2BH88; -.
DR STRING; 525254.HMPREF0072_1708; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_4_9; -.
DR Proteomes; UP000005984; Unassembled WGS sequence.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
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; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:EEI85731.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005984}.
FT DOMAIN 2..125
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 127 AA; 15114 MW; 4A0C5629464BBDB5 CRC64;
MKFLHTMVRV KDLEKSFKFY TEELGFVESR RREFPEKKFD LVYLMLPGSP DYELELTYNY
DQEEGYEIGT GYGHIAISHP DIYTLREALM KKGYEVTEIR GLTPNSNKYF FVTDPDGYRI
EIIQKED
//
