Q9AGP8 (Q9AGP8_ARTGO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
N,N-dimethylglycine oxidase EMBL AAK16482.1

Gene names

Name:

dmg EMBL AAK16482.1

Organism

Arthrobacter globiformis EMBL AAK16482.1

Taxonomic identifier

1665 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	830 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the GcvT family. RuleBase RU003980

Ontologies

Keywords
Ligand	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI Flavoprotein PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI Nucleotide-binding PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
Technical term	3D-structure PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
Gene Ontology (GO)
Biological_process	glycine catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	aminomethyltransferase activity Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	14 – 15	2	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Nucleotide binding	35 – 36	2	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Nucleotide binding	45 – 48	4	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Nucleotide binding	360 – 363	4	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Region	658 – 660	3	Tetrahydrofolic acid binding PDB 3GSI
Sites
	Binding site	52	1	FAD; via amide nitrogen and carbonyl oxygen PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Binding site	174	1	FAD; via amide nitrogen and carbonyl oxygen PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Binding site	206	1	FAD PDB 1PJ5 PDB 1PJ6 PDB 1PJ7 PDB 3GSI
	Binding site	259	1	FAD PDB 1PJ6
	Binding site	335	1	FAD PDB 1PJ5
	Binding site	539	1	Tetrahydrofolic acid PDB 3GSI
	Binding site	554	1	Tetrahydrofolic acid PDB 3GSI
	Binding site	566	1	Tetrahydrofolic acid; via carbonyl oxygen PDB 3GSI
	Binding site	632	1	Tetrahydrofolic acid PDB 3GSI
	Binding site	699	1	Tetrahydrofolic acid PDB 3GSI
	Site	225	1	Important for catalytic activity PDB 1PJ5
	Site	259	1	Important for catalytic activity PDB 1PJ5
	Site	552	1	Important for catalytic activity PDB 1PJ5

Sequences

	Sequence		Length	Mass (Da)
	Q9AGP8 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 13DE3C4B3DF325DA	FASTA	830	89,985
	10 20 30 40 50 60 MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP GLVFQTNPSK 70 80 90 100 110 120 TMASFAKYTV EKLLSLTEDG VSCFNQVGGL EVATTETRLA DLKRKLGYAA AWGIEGRLLS 130 140 150 160 170 180 PAECQELYPL LDGENILGGL HVPSDGLASA ARAVQLLIKR TESAGVTYRG STTVTGIEQS 190 200 210 220 230 240 GGRVTGVQTA DGVIPADIVV SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN 250 260 270 280 290 300 DQPNGARLPI LRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR 310 320 330 340 350 360 LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPD GGPLLGESKE LDGFYVAEAV 370 380 390 400 410 420 WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP EYVSETSQQN FVEIYDVLHP 430 440 450 460 470 480 LQPRLSPRNL RVSPFHARHK ELGAFFLEAG GWERPYWFEA NAALLKEMPA EWLPPARDAW 490 500 510 520 530 540 SGMFSSPIAA AEAWKTRTAV AMYDMTPLKR LEVSGPGALK LLQELTTADL AKKPGAVTYT 550 560 570 580 590 600 LLLDHAGGVR SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG 610 620 630 640 650 660 GTCCIGLWGP LARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS YVGELGWELY 670 680 690 700 710 720 TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYR SWGTDMTTEH DPFEAGLGFA 730 740 750 760 770 780 VKMAKESFIG KGALEGRTEE ASARRLRCLT IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG 790 800 810 820 830 YTVAKPIAYS YLPGTVSVGD SVDIEYFGRR ITATVTEDPL YDPKMTRLRG

References

[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. Strain: NRRL B-2979 EMBL AAK16482.1.
[2]	"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, ACTIVE SITE.
[3]	"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 TETRAHYDROFOLIC ACID.
[4]	"Arthrobacter globiformis N,N-dimethylglycine oxidase operon." Casaite V., Bruzyte S., Meskys R. Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: NRRL B-2979 EMBL AAK16482.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF329477 Genomic DNA. Translation: AAK16482.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9AGP8.

SMR

Q9AGP8. Positions 3-830.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Enzyme and pathway databases

BRENDA

1.5.3.10. 1012.

Family and domain databases

Gene3D

3.30.1360.120. 2 hits.

InterPro

IPR006076. FAD-dep_OxRdtase.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]

Pfam

PF01266. DAO. 1 hit.
PF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9AGP8.

Entry information

Entry name

Q9AGP8_ARTGO

Accession

Primary (citable) accession number: Q9AGP8

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)