GR_BACSU
ID GR_BACSU Reviewed; 276 AA.
AC O32210; Q7B2L2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glyoxal reductase;
DE Short=GR;
DE EC=1.1.1.-;
DE AltName: Full=Methylglyoxal reductase;
DE EC=1.1.1.283;
GN Name=yvgN; OrderedLocusNames=BSU33400;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-31, AND FUNCTION.
RC STRAIN=CRK6000, and IFO 3007;
RX PubMed=16232966; DOI=10.1263/jbb.91.147;
RA Sakai A., Katayama K., Katsuragi T., Tani Y.;
RT "Glycolaldehyde-forming route in Bacillus subtilis in relation to vitamin
RT B6 biosynthesis.";
RL J. Biosci. Bioeng. 91:147-152(2001).
CC -!- FUNCTION: Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not
CC involved in the vitamin B6 biosynthesis. {ECO:0000269|PubMed:16232966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH;
CC Xref=Rhea:RHEA:21748, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158,
CC ChEBI:CHEBI:18041, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.283;
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AJ223978; CAA11712.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15345.1; -; Genomic_DNA.
DR PIR; C70040; C70040.
DR RefSeq; NP_391220.1; NC_000964.3.
DR RefSeq; WP_003243374.1; NZ_JNCM01000033.1.
DR PDB; 3D3F; X-ray; 2.40 A; A/B=2-276.
DR PDB; 3F7J; X-ray; 1.70 A; A/B=1-276.
DR PDBsum; 3D3F; -.
DR PDBsum; 3F7J; -.
DR AlphaFoldDB; O32210; -.
DR SMR; O32210; -.
DR IntAct; O32210; 1.
DR MINT; O32210; -.
DR STRING; 224308.BSU33400; -.
DR jPOST; O32210; -.
DR PaxDb; O32210; -.
DR PRIDE; O32210; -.
DR EnsemblBacteria; CAB15345; CAB15345; BSU_33400.
DR GeneID; 936001; -.
DR KEGG; bsu:BSU33400; -.
DR PATRIC; fig|224308.179.peg.3625; -.
DR eggNOG; COG0656; Bacteria.
DR InParanoid; O32210; -.
DR OMA; FMTMKAA; -.
DR PhylomeDB; O32210; -.
DR BioCyc; BSUB:BSU33400-MON; -.
DR BioCyc; MetaCyc:BSU33400-MON; -.
DR EvolutionaryTrace; O32210; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) activity; IEA:UniProtKB-EC.
DR CDD; cd19157; AKR_AKR5G1-3; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044500; AKR5G.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; PTHR43827; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16232966"
FT CHAIN 2..276
FT /note="Glyoxal reductase"
FT /id="PRO_0000360642"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190..242
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3F7J"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:3F7J"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3F7J"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:3F7J"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:3F7J"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:3F7J"
SQ SEQUENCE 276 AA; 31663 MW; 3EDB1F384BB77AC0 CRC64;
MPTSLKDTVK LHNGVEMPWF GLGVFKVENG NEATESVKAA IKNGYRSIDT AAIYKNEEGV
GIGIKESGVA REELFITSKV WNEDQGYETT LAAFEKSLER LQLDYLDLYL IHWPGKDKYK
DTWRALEKLY KDGKIRAIGV SNFQVHHLEE LLKDAEIKPM VNQVEFHPRL TQKELRDYCK
GQGIQLEAWS PLMQGQLLDN EVLTQIAEKH NKSVAQVILR WDLQHGVVTI PKSIKEHRII
ENADIFDFEL SQEDMDKIDA LNKDERVGPN PDELLF
