Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9AGP8

- DMGO_ARTGO

UniProt

Q9AGP8 - DMGO_ARTGO

Protein

Dimethylglycine oxidase

Gene

dmg

Organism
Arthrobacter globiformis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the oxidative demethylation of N,N-dimethylglycine to yield sarcosine, formaldehyde and hydrogen peroxide. The oxidation of dimethylglycine is coupled to the synthesis of 5,10-methylenetetrahydrofolate through an unusual substrate channeling mechanism. This channeling occurs by nonbiased diffusion of the iminium intermediate through a large solvent cavity connecting active site 1 (N-terminus) and active site 2 (C-terminus). The synthesis of 5,10-methylenetetrahydrofolate (at active site 2) prevents the accumulation of formaldehyde, formed by hydrolysis of the iminium intermediate product (at active site 1). Does not oxidize sarcosine.4 Publications

    Catalytic activityi

    N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2.1 Publication
    N,N-dimethylglycine + tetrahydrofolate = sarcosine + 5,10-methylenetetrahydrofolate.1 Publication

    Cofactori

    Binds 1 FAD per subunit.2 Publications

    Kineticsi

    1. KM=2 mM for N,N-dimethylglycine1 Publication

    pH dependencei

    Optimum pH is 8.0-10.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei174 – 1741FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Active sitei225 – 2251Sequence Analysis
    Sitei225 – 2251Important for catalytic activity
    Active sitei259 – 2591Sequence Analysis
    Binding sitei259 – 2591FAD2 Publications
    Sitei259 – 2591Important for catalytic activity
    Active sitei552 – 5521For 5,10-methylenetetrahydrofolate synthesis activitySequence Analysis
    Sitei552 – 5521Important for catalytic activity
    Binding sitei554 – 5541Tetrahydrofolic acid
    Binding sitei566 – 5661Tetrahydrofolic acid; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 152FAD2 Publications
    Nucleotide bindingi35 – 362FAD2 Publications
    Nucleotide bindingi45 – 484FAD2 Publications
    Nucleotide bindingi360 – 3634FAD2 Publications

    GO - Molecular functioni

    1. aminomethyltransferase activity Source: InterPro
    2. dimethylglycine oxidase activity Source: UniProtKB-EC
    3. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. glycine catabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi1.5.3.10. 1012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethylglycine oxidase (EC:1.5.3.10)
    Short name:
    DMGO
    Gene namesi
    Name:dmg
    OrganismiArthrobacter globiformis
    Taxonomic identifieri1665 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi225 – 2251H → Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold. 1 Publication
    Mutagenesisi259 – 2591Y → F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold. 1 Publication
    Mutagenesisi552 – 5521D → A: No effect on the activity. 1 Publication
    Mutagenesisi552 – 5521D → N: Reduces activity 3-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 830830Dimethylglycine oxidasePRO_0000428956Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Pros-8alpha-FAD histidine

    Structurei

    Secondary structure

    1
    830
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Helixi14 – 2512
    Beta strandi31 – 344
    Helixi45 – 473
    Helixi60 – 7516
    Beta strandi81 – 855
    Beta strandi89 – 957
    Helixi96 – 11217
    Beta strandi117 – 1193
    Helixi121 – 1277
    Helixi133 – 1353
    Beta strandi138 – 1425
    Beta strandi146 – 1483
    Helixi150 – 16314
    Beta strandi167 – 1693
    Beta strandi174 – 1807
    Beta strandi183 – 1897
    Beta strandi192 – 1954
    Beta strandi197 – 2015
    Helixi204 – 2063
    Helixi207 – 2126
    Turni213 – 2153
    Beta strandi221 – 23111
    Helixi234 – 2363
    Turni237 – 2393
    Turni242 – 2443
    Beta strandi250 – 2534
    Helixi254 – 2563
    Beta strandi258 – 2636
    Beta strandi266 – 2716
    Helixi281 – 2833
    Helixi289 – 2913
    Helixi305 – 31814
    Helixi320 – 3245
    Beta strandi327 – 33711
    Beta strandi344 – 3474
    Beta strandi349 – 3524
    Beta strandi354 – 3596
    Helixi362 – 3643
    Helixi365 – 37814
    Turni386 – 3883
    Helixi390 – 3923
    Helixi395 – 3984
    Helixi400 – 41213
    Turni413 – 4153
    Beta strandi425 – 4273
    Helixi436 – 4416
    Beta strandi444 – 4496
    Beta strandi452 – 4587
    Helixi459 – 4679
    Helixi470 – 4723
    Helixi479 – 4824
    Helixi488 – 49811
    Beta strandi501 – 5044
    Beta strandi510 – 5156
    Helixi518 – 5258
    Beta strandi526 – 5283
    Beta strandi536 – 5438
    Beta strandi549 – 55911
    Beta strandi562 – 5665
    Helixi570 – 58617
    Beta strandi594 – 5974
    Helixi599 – 6013
    Beta strandi602 – 6098
    Helixi612 – 6165
    Turni617 – 6193
    Turni626 – 6283
    Beta strandi633 – 6397
    Beta strandi642 – 6476
    Beta strandi653 – 66210
    Helixi663 – 67715
    Helixi678 – 6803
    Beta strandi683 – 6853
    Helixi687 – 69610
    Turni702 – 7043
    Turni712 – 7165
    Helixi718 – 7203
    Helixi731 – 7344
    Turni739 – 7413
    Beta strandi743 – 7519
    Beta strandi763 – 7664
    Beta strandi769 – 7735
    Beta strandi776 – 7805
    Turni781 – 7844
    Beta strandi785 – 7939
    Beta strandi801 – 8066
    Beta strandi809 – 8168
    Turni826 – 8283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PJ5X-ray1.61A1-830[»]
    1PJ6X-ray1.65A1-830[»]
    1PJ7X-ray2.10A1-830[»]
    3GSIX-ray2.00A4-830[»]
    ProteinModelPortaliQ9AGP8.
    SMRiQ9AGP8. Positions 3-830.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9AGP8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni658 – 6603Tetrahydrofolic acid binding

    Sequence similaritiesi

    Belongs to the GcvT family.Curated

    Family and domain databases

    Gene3Di2.40.30.110. 1 hit.
    3.30.1360.120. 2 hits.
    InterProiIPR006076. FAD-dep_OxRdtase.
    IPR013977. GCV_T_C.
    IPR006222. GCV_T_N.
    IPR029043. GcvT/YgfZ_C.
    IPR027266. TrmE/GcvT_dom1.
    [Graphical view]
    PfamiPF01266. DAO. 1 hit.
    PF01571. GCV_T. 1 hit.
    PF08669. GCV_T_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF101790. SSF101790. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9AGP8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP    50
    GLVFQTNPSK TMASFAKYTV EKLLSLTEDG VSCFNQVGGL EVATTETRLA 100
    DLKRKLGYAA AWGIEGRLLS PAECQELYPL LDGENILGGL HVPSDGLASA 150
    ARAVQLLIKR TESAGVTYRG STTVTGIEQS GGRVTGVQTA DGVIPADIVV 200
    SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN DQPNGARLPI 250
    LRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR 300
    LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPD GGPLLGESKE 350
    LDGFYVAEAV WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP 400
    EYVSETSQQN FVEIYDVLHP LQPRLSPRNL RVSPFHARHK ELGAFFLEAG 450
    GWERPYWFEA NAALLKEMPA EWLPPARDAW SGMFSSPIAA AEAWKTRTAV 500
    AMYDMTPLKR LEVSGPGALK LLQELTTADL AKKPGAVTYT LLLDHAGGVR 550
    SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG 600
    GTCCIGLWGP LARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS 650
    YVGELGWELY TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYR 700
    SWGTDMTTEH DPFEAGLGFA VKMAKESFIG KGALEGRTEE ASARRLRCLT 750
    IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG YTVAKPIAYS YLPGTVSVGD 800
    SVDIEYFGRR ITATVTEDPL YDPKMTRLRG 830
    Length:830
    Mass (Da):89,985
    Last modified:June 1, 2001 - v1
    Checksum:i13DE3C4B3DF325DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF329477 Genomic DNA. Translation: AAK16482.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF329477 Genomic DNA. Translation: AAK16482.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PJ5 X-ray 1.61 A 1-830 [» ]
    1PJ6 X-ray 1.65 A 1-830 [» ]
    1PJ7 X-ray 2.10 A 1-830 [» ]
    3GSI X-ray 2.00 A 4-830 [» ]
    ProteinModelPortali Q9AGP8.
    SMRi Q9AGP8. Positions 3-830.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 1.5.3.10. 1012.

    Miscellaneous databases

    EvolutionaryTracei Q9AGP8.

    Family and domain databases

    Gene3Di 2.40.30.110. 1 hit.
    3.30.1360.120. 2 hits.
    InterProi IPR006076. FAD-dep_OxRdtase.
    IPR013977. GCV_T_C.
    IPR006222. GCV_T_N.
    IPR029043. GcvT/YgfZ_C.
    IPR027266. TrmE/GcvT_dom1.
    [Graphical view ]
    Pfami PF01266. DAO. 1 hit.
    PF01571. GCV_T. 1 hit.
    PF08669. GCV_T_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101790. SSF101790. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism."
      Meskys R., Harris R.J., Casaite V., Basran J., Scrutton N.S.
      Eur. J. Biochem. 268:3390-3398(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NRRL B-2979.
    2. "Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry."
      Basran J., Bhanji N., Basran A., Nietlispach D., Mistry S., Meskys R., Scrutton N.S.
      Biochemistry 41:4733-4743(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-58, FUNCTION, FAD-BINDING AT HIS-48.
      Strain: NRRL B-2979.
    3. "Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase."
      Leys D., Basran J., Scrutton N.S.
      EMBO J. 22:4038-4048(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) IN COMPLEX WITH FAD AND TETRAHYDROFOLATE, FUNCTION, MUTAGENESIS OF HIS-225 AND TYR-259.
      Strain: NRRL B-2979.
    4. "An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde."
      Tralau T., Lafite P., Levy C., Combe J.P., Scrutton N.S., Leys D.
      J. Biol. Chem. 284:17826-17834(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 4-830 IN COMPLEX WITH FAD AND TETRAHYDROFOLATE, FUNCTION, MUTAGENESIS OF ASP-552.
      Strain: NRRL B-2979.

    Entry informationi

    Entry nameiDMGO_ARTGO
    AccessioniPrimary (citable) accession number: Q9AGP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 66 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3