Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glyoxal reductase

Gene

yvgN

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis.1 Publication

Catalytic activityi

(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541Proton donorBy similarity
Binding sitei112 – 1121SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 24253NADPBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU33400-MONOMER.
RETL1328306-WGS:GSTH-2828-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxal reductase (EC:1.1.1.-)
Short name:
GR
Alternative name(s):
Methylglyoxal reductase (EC:1.1.1.283)
Gene namesi
Name:yvgN
Ordered Locus Names:BSU33400
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 276275Glyoxal reductasePRO_0000360642Add
BLAST

Proteomic databases

PaxDbiO32210.

Interactioni

Protein-protein interaction databases

IntActiO32210. 1 interaction.
MINTiMINT-8367019.
STRINGi224308.Bsubs1_010100018136.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi16 – 205Combined sources
Helixi31 – 4212Combined sources
Beta strandi47 – 493Combined sources
Helixi52 – 543Combined sources
Helixi57 – 6711Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 806Combined sources
Helixi82 – 843Combined sources
Helixi87 – 10115Combined sources
Beta strandi106 – 1127Combined sources
Turni115 – 1173Combined sources
Helixi119 – 13113Combined sources
Beta strandi134 – 1429Combined sources
Helixi145 – 15410Combined sources
Beta strandi160 – 1656Combined sources
Helixi173 – 18210Combined sources
Beta strandi185 – 1906Combined sources
Helixi193 – 1953Combined sources
Turni196 – 1994Combined sources
Helixi201 – 21010Combined sources
Helixi214 – 22411Combined sources
Helixi236 – 2427Combined sources
Helixi252 – 2598Combined sources
Turni271 – 2733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D3FX-ray2.40A/B2-276[»]
3F7JX-ray1.70A/B1-276[»]
ProteinModelPortaliO32210.
SMRiO32210. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32210.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656. LUCA.
HOGENOMiHOG000250272.
InParanoidiO32210.
OMAiMLMIEAN.
OrthoDBiEOG68H8C2.
PhylomeDBiO32210.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O32210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTSLKDTVK LHNGVEMPWF GLGVFKVENG NEATESVKAA IKNGYRSIDT
60 70 80 90 100
AAIYKNEEGV GIGIKESGVA REELFITSKV WNEDQGYETT LAAFEKSLER
110 120 130 140 150
LQLDYLDLYL IHWPGKDKYK DTWRALEKLY KDGKIRAIGV SNFQVHHLEE
160 170 180 190 200
LLKDAEIKPM VNQVEFHPRL TQKELRDYCK GQGIQLEAWS PLMQGQLLDN
210 220 230 240 250
EVLTQIAEKH NKSVAQVILR WDLQHGVVTI PKSIKEHRII ENADIFDFEL
260 270
SQEDMDKIDA LNKDERVGPN PDELLF
Length:276
Mass (Da):31,663
Last modified:January 1, 1998 - v1
Checksum:i3EDB1F384BB77AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11712.1.
AL009126 Genomic DNA. Translation: CAB15345.1.
PIRiC70040.
RefSeqiNP_391220.1. NC_000964.3.
WP_003243374.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15345; CAB15345; BSU33400.
GeneIDi936001.
KEGGibsu:BSU33400.
PATRICi18978680. VBIBacSub10457_3503.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11712.1.
AL009126 Genomic DNA. Translation: CAB15345.1.
PIRiC70040.
RefSeqiNP_391220.1. NC_000964.3.
WP_003243374.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D3FX-ray2.40A/B2-276[»]
3F7JX-ray1.70A/B1-276[»]
ProteinModelPortaliO32210.
SMRiO32210. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO32210. 1 interaction.
MINTiMINT-8367019.
STRINGi224308.Bsubs1_010100018136.

Proteomic databases

PaxDbiO32210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15345; CAB15345; BSU33400.
GeneIDi936001.
KEGGibsu:BSU33400.
PATRICi18978680. VBIBacSub10457_3503.

Phylogenomic databases

eggNOGiCOG0656. LUCA.
HOGENOMiHOG000250272.
InParanoidiO32210.
OMAiMLMIEAN.
OrthoDBiEOG68H8C2.
PhylomeDBiO32210.

Enzyme and pathway databases

BioCyciBSUB:BSU33400-MONOMER.
RETL1328306-WGS:GSTH-2828-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32210.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
    Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
    Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Glycolaldehyde-forming route in Bacillus subtilis in relation to vitamin B6 biosynthesis."
    Sakai A., Katayama K., Katsuragi T., Tani Y.
    J. Biosci. Bioeng. 91:147-152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31, FUNCTION.
    Strain: CRK6000 and IFO 3007.

Entry informationi

Entry nameiGR_BACSU
AccessioniPrimary (citable) accession number: O32210
Secondary accession number(s): Q7B2L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.