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Database: UniProt
Entry: R5UEW2_9BACT
LinkDB: R5UEW2_9BACT
Original site: R5UEW2_9BACT 
ID   R5UEW2_9BACT            Unreviewed;       283 AA.
AC   R5UEW2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Glyoxal reductase {ECO:0000313|EMBL:CCZ76808.1};
GN   ORFNames=BN754_02316 {ECO:0000313|EMBL:CCZ76808.1};
OS   Alistipes finegoldii CAG:68.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1263035 {ECO:0000313|EMBL:CCZ76808.1, ECO:0000313|Proteomes:UP000018154};
RN   [1] {ECO:0000313|EMBL:CCZ76808.1, ECO:0000313|Proteomes:UP000018154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:68 {ECO:0000313|Proteomes:UP000018154};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ76808.1}.
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DR   EMBL; CBAO010000219; CCZ76808.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UEW2; -.
DR   Proteomes; UP000018154; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd19133; AKR_AKR5F1; 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;
FT   DOMAIN          28..256
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        48
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            73
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ   SEQUENCE   283 AA;  31984 MW;  F260EAE80432FA97 CRC64;
     MEHRILNNGV EMPVLGFGVY QVGETVCEQC VRDAIAAGYR SIDTASAYLN ERAVGRAIRR
     SGVPREELFI TTKLWVQDAG YESTKRAFAK SLERLQLDYL DLYLIHQPFG DVYGSWRAME
     ELYREGAVRA IGVSNFQPDR LVDLILHNEV VPAVNQVETH PFCQQTEAAA VMASEGVQIE
     SWAPFAEGRN NLFGNGTLVS LAAKYRKSVA QVVLRWLIQR GVVVIPKSVR PERMAENIAV
     FDFHLAPEDM DLIATLDTRR SCFLSHRDPE TVKWLGTMKY EMD
//
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