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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)DescriptionActionsGraphical viewLength
Active sitei54Proton donorBy similarity1
Binding sitei112SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi190 – 242NADPBy similarityAdd BLAST53

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU33400-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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003606422 – 276Glyoxal reductaseAdd BLAST275

Proteomic databases

PaxDbiO32210.
PRIDEiO32210.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Beta strandi16 – 20Combined sources5
Helixi31 – 42Combined sources12
Beta strandi47 – 49Combined sources3
Helixi52 – 54Combined sources3
Helixi57 – 67Combined sources11
Helixi71 – 73Combined sources3
Beta strandi75 – 80Combined sources6
Helixi82 – 84Combined sources3
Helixi87 – 101Combined sources15
Beta strandi106 – 112Combined sources7
Turni115 – 117Combined sources3
Helixi119 – 131Combined sources13
Beta strandi134 – 142Combined sources9
Helixi145 – 154Combined sources10
Beta strandi160 – 165Combined sources6
Helixi173 – 182Combined sources10
Beta strandi185 – 190Combined sources6
Helixi193 – 195Combined sources3
Turni196 – 199Combined sources4
Helixi201 – 210Combined sources10
Helixi214 – 224Combined sources11
Helixi236 – 242Combined sources7
Helixi252 – 259Combined sources8
Turni271 – 273Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO32210.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656. LUCA.
HOGENOMiHOG000250272.
InParanoidiO32210.
OMAiIQENFAV.
PhylomeDBiO32210.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D3FX-ray2.40A/B2-276[»]
3F7JX-ray1.70A/B1-276[»]
ProteinModelPortaliO32210.
SMRiO32210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiO32210.
PRIDEiO32210.

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.
OMAiIQENFAV.
PhylomeDBiO32210.

Enzyme and pathway databases

BioCyciBSUB:BSU33400-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32210.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
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...

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: November 2, 2016
This is version 97 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.