Reviewed, UniProtKB/Swiss-Prot Q53062 (MEDH_RHOER)

Names and origin

Protein names

Recommended name:
    NDMA-dependent methanol dehydrogenase
    EC=1.1.99.-

Gene names

Name:

thcE

Organism

Rhodococcus erythropolis

Taxonomic identifier

1833 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of alcohols (including methanol) with the concomitant reduction of N,N'-dimethyl-4-nitroso-aniline (NDMA), aldehydes or ketones. Ref.2
Catalytic activity	Alcohol + NDMAH = aldehyde + NDMA+. Ref.2
Cofactor	NADPH. Ref.2
Subcellular location	Cytoplasm. Ref.2
Induction	Expressed during degradation of thiocarbamates and atrazine. Ref.1
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	NDMA-dependent methanol dehydrogenase		PRO_0000247755

Sequences

	Sequence		Length	Mass (Da)
	Q53062-1 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: 5DB811D6BFDDA820	FASTA	423	46,356
	10 20 30 40 50 60 AIELNQIWDF PIKEFHPFPR ALMGVGAHDI IGVEAKNLGF KRTLLMTTGL RGSGIIEELV 70 80 90 100 110 120 GKIEYQGVEV VLYDKVESNP KDYNVMEAAA LYQKEKCDSI ISIGGGSSHD AAKGARVVIA 130 140 150 160 170 180 HDGRNINEFE GFAKSTNKEN PPHIAVSTTA GTGSETSWAY VITDTSDMNN PHKWVGFDEA 190 200 210 220 230 240 TIVTLAIDDP LLYYTCPQHF TAYCGFDVLA HGSEPFVSRL DFAPSLGNAI YSVELVAKNL 250 260 270 280 290 300 REAVFEPRNL KAREGMMNAQ YIAGQAFNSG GLGIVHSISH AVSAFFDSHH GLNNAIALPR 310 320 330 340 350 360 VWEYNLPSRY ERYAQLAGAL GVDTRNLTTV QAADAAVEAA IRLAKDVGIP DNFGQVRTDS 370 380 390 400 410 420 YAKNQMNTKK YEGRGDVIKG DEKTVRAISE HIQDDWCTPG NPREVTVESM IPVVDHAINK SYF

References

[1]

"Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol:N,N'-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides." Nagy I., Verheijen S., De Schrijver A., Van Damme J., Proost P., Schoofs G., Vanderleyden J., De Mot R. Arch. Microbiol. 163:439-446(1995) [PubMed: 7575099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19; 88-105 AND 180-195, INDUCTION. Strain: NI86/21.

[2]

"Methanol:NDMA oxidoreductase from Rhodococcus erythropolis DSM 1069." Schenkels P., Piersma S.R., Duine J.A. Submitted (JUL-1999) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION. Strain: DSM 1069.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U21071 Genomic DNA. Translation: AAB80771.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view]
Pfam	PF00465. Fe-ADH. 1 hit. [Graphical view]
PROSITE	PS00913. ADH_IRON_1. False negative. PS00060. ADH_IRON_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MEDH_RHOER

Accession

Primary (citable) accession number: Q53062
Secondary accession number(s): P81938

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	June 16, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)