GS69_BACSU
ID GS69_BACSU Reviewed; 331 AA.
AC P80874; O07583;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Aldo-keto reductase YhdN {ECO:0000305|PubMed:12554958};
DE EC=1.1.1.- {ECO:0000269|PubMed:12554958, ECO:0000269|PubMed:15019785};
DE AltName: Full=AKR11B {ECO:0000303|PubMed:12554958};
DE AltName: Full=General stress protein 69 {ECO:0000303|PubMed:9298659};
DE Short=GSP69 {ECO:0000303|PubMed:9298659};
GN Name=yhdN; OrderedLocusNames=BSU09530;
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=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(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 1-25, AND INDUCTION.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=12554958; DOI=10.1107/s0907444902072001;
RA Ehrensberger A., Wilson D.K.;
RT "Expression, crystallization and activities of the two family 11 aldo-keto
RT reductases from Bacillus subtilis.";
RL Acta Crystallogr. D 59:375-377(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=15019785; DOI=10.1016/j.jmb.2004.01.059;
RA Ehrensberger A.H., Wilson D.K.;
RT "Structural and catalytic diversity in the two family 11 aldo-keto
RT reductases.";
RL J. Mol. Biol. 337:661-673(2004).
CC -!- FUNCTION: Aldo-keto reductase (AKR) that displays broad substrate
CC specificity in vitro. Is able to reduce the standard AKR substrates DL-
CC glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde,
CC benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use
CC NADH as a cosubstrate. Does not act on glucose, 2-pyridine
CC carboxyaldehyde, fructose and xylose. The physiological function of
CC this enzyme is not clear. May play a role in bacterial stress response
CC and/or in detoxification of reactive aldehydes.
CC {ECO:0000269|PubMed:12554958, ECO:0000269|PubMed:15019785}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for DL-glyceraldehyde {ECO:0000269|PubMed:12554958};
CC KM=0.67 mM for p-nitrobenzaldehyde {ECO:0000269|PubMed:12554958};
CC KM=12.2 uM for NADPH {ECO:0000269|PubMed:12554958};
CC KM=0.54 mM for D-erythrose {ECO:0000269|PubMed:15019785};
CC KM=0.74 mM for methylglyoxal {ECO:0000269|PubMed:15019785};
CC KM=1.91 mM for benzaldehyde {ECO:0000269|PubMed:15019785};
CC KM=1.51 mM for butyraldehyde {ECO:0000269|PubMed:15019785};
CC Note=kcat is 1.37 sec(-1) with DL-glyceraldehyde as substrate
CC (PubMed:12554958). kcat is 1.09 sec(-1) with p-nitrobenzaldehyde as
CC substrate (PubMed:12554958). kcat is 4.02 sec(-1) with D-erythrose as
CC substrate (PubMed:15019785). kcat is 5.33 sec(-1) with methylglyoxal
CC as substrate (PubMed:15019785). kcat is 2.59 sec(-1) with
CC benzaldehyde as substrate (PubMed:15019785). kcat is 3.96 sec(-1)
CC with butyraldehyde as substrate (PubMed:15019785).
CC {ECO:0000269|PubMed:12554958, ECO:0000269|PubMed:15019785};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12554958}.
CC -!- INDUCTION: Is under the control of the sigma-B transcription factor. Is
CC induced by heat shock, salt stress, oxidative stress, glucose
CC limitation and oxygen limitation. {ECO:0000269|PubMed:9298659}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 11 subfamily. {ECO:0000305|PubMed:12554958}.
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DR EMBL; Y14082; CAA74498.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12792.1; -; Genomic_DNA.
DR PIR; D69826; D69826.
DR RefSeq; NP_388834.1; NC_000964.3.
DR RefSeq; WP_003245422.1; NZ_JNCM01000035.1.
DR PDB; 1PZ1; X-ray; 2.20 A; A/B=1-331.
DR PDBsum; 1PZ1; -.
DR AlphaFoldDB; P80874; -.
DR SMR; P80874; -.
DR STRING; 224308.BSU09530; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR TCDB; 8.A.5.1.4; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR PaxDb; P80874; -.
DR PRIDE; P80874; -.
DR EnsemblBacteria; CAB12792; CAB12792; BSU_09530.
DR GeneID; 939270; -.
DR KEGG; bsu:BSU09530; -.
DR PATRIC; fig|224308.179.peg.1026; -.
DR eggNOG; COG0667; Bacteria.
DR InParanoid; P80874; -.
DR OMA; ISAQNHY; -.
DR PhylomeDB; P80874; -.
DR BioCyc; BSUB:BSU09530-MON; -.
DR SABIO-RK; P80874; -.
DR EvolutionaryTrace; P80874; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 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 Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome; Stress response.
FT CHAIN 1..331
FT /note="Aldo-keto reductase YhdN"
FT /id="PRO_0000070388"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15019785"
FT BINDING 20..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 203..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 280..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT BINDING 286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785,
FT ECO:0007744|PDB:1PZ1"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000305|PubMed:15019785"
FT CONFLICT 25
FT /note="G -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1PZ1"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1PZ1"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 238..256
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1PZ1"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:1PZ1"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1PZ1"
SQ SEQUENCE 331 AA; 37312 MW; 82BC24D46E4994D0 CRC64;
MEYTSIADTG IEASRIGLGT WAIGGTMWGG TDEKTSIETI RAALDQGITL IDTAPAYGFG
QSEEIVGKAI KEYGKRDQVI LATKTALDWK NNQLFRHANR ARIVEEVENS LKRLQTDYID
LYQVHWPDPL VPIEETAEVM KELYDAGKIR AIGVSNFSIE QMDTFRAVAP LHTIQPPYNL
FEREMEESVL PYAKDNKITT LLYGSLCRGL LTGKMTEEYT FEGDDLRNHD PKFQKPRFKE
YLSAVNQLDK LAKTRYGKSV IHLAVRWILD QPGADIALWG ARKPGQLEAL SEITGWTLNS
EDQKDINTIL ENTISDPVGP EFMAPPTREE I
