P22619 (DHML_PARDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylamine dehydrogenase light chain
Short name=MADH
EC=1.4.9.1

Alternative name(s):
Methylamine dehydrogenase (amicyanin)

Gene names

Name:

mauA

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
Catalytic activity	Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin.
Cofactor	Contains 1 tryptophan tryptophylquinone per subunit.
Pathway	One-carbon metabolism; methylamine degradation; formaldehyde from methylamine: step 1/1.
Subunit structure	Heterotetramer of two light and two heavy chains.
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.
Sequence similarities	Belongs to the aromatic amine dehydrogenase light chain family.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond TTQ
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	amine metabolic process Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular_function	amine dehydrogenase activity Inferred from electronic annotation. Source: InterPro methylamine dehydrogenase (amicyanin) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 57

57

Tat-type signal Potential

Chain

58 – 188

131

Methylamine dehydrogenase light chain

PRO_0000025575

Amino acid modifications

Modified residue

114

1

Tryptophylquinone Ref.3

Disulfide bond

80 ↔ 145

Disulfide bond

86 ↔ 118

Disulfide bond

93 ↔ 178

Disulfide bond

95 ↔ 143

Disulfide bond

103 ↔ 134

Disulfide bond

135 ↔ 166

Cross-link

114 ↔ 165

Tryptophan tryptophylquinone (Trp-Trp) Ref.3

Secondary structure

1

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188

Helix Strand Turn

Details...

Beta strand

66 – 68

3

Beta strand

73 – 75

3

Helix

83 – 85

3

Beta strand

89 – 92

4

Helix

93 – 96

4

Beta strand

100 – 103

4

Beta strand

114 – 120

7

Turn

121 – 124

4

Beta strand

125 – 137

13

Beta strand

142 – 146

5

Helix

157 – 159

3

Beta strand

161 – 163

3

Helix

170 – 172

3

Beta strand

175 – 180

6

Beta strand

183 – 185

3

Sequences

	Sequence		Length	Mass (Da)
	P22619 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: E3D9DE4454268BE8	FASTA	188	20,393
	10 20 30 40 50 60 MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG RVSRANAADA 70 80 90 100 110 120 PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN 130 140 150 160 170 180 PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI SPIVGKAS

References

[1]	"The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans." Chistoserdov A.Y., Boyd J., Mathews F.S., Lidstrom M.E. Biochem. Biophys. Res. Commun. 184:1181-1189(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation." van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H. FEBS Lett. 275:217-220(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-188. Strain: ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785.
[3]	"Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8-A resolution." Chen L., Mathews F.S., Davidson V.L., Huizinga E.G., Vellieux F.M.D., Hol W.G.J. Proteins 14:288-299(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 64-188.
[4]	"Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin." Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J. Biochemistry 31:4959-4964(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 64-188 IN COMPLEX WITH AMICYANIN.
[5]	"Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i." Chen L., Durley R., Mathews F.S., Davidson V.L. Science 264:86-90(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M90098 Genomic DNA. Translation: AAA25578.1.
X55665 Genomic DNA. Translation: CAA39198.1.

PIR

JH0661.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MG2	X-ray	2.25	B/F/J/N	58-188	[»]
1MG3	X-ray	2.40	B/F/J/N	58-188	[»]
2BBK	X-ray	1.75	L/M	64-188	[»]
2GC4	X-ray	1.90	B/F/J/N	58-188	[»]
2GC7	X-ray	1.90	B/F/J/N	58-188	[»]
2J55	X-ray	2.15	L/M	58-188	[»]
2J56	X-ray	2.10	L/M	58-188	[»]
2J57	X-ray	2.25	K/L/M/N	58-188	[»]
2MTA	X-ray	2.40	L	64-188	[»]
3ORV	X-ray	1.91	C/E	58-188	[»]
3PXS	X-ray	2.22	C/E	58-188	[»]
3PXT	X-ray	2.16	C/E	58-188	[»]
3PXW	X-ray	2.11	C/E	58-188	[»]
3RLM	X-ray	2.13	C/E	58-188	[»]
3RMZ	X-ray	1.72	C/E	58-188	[»]
3RN0	X-ray	1.91	C/E	58-188	[»]
4FA1	X-ray	2.18	C/E	58-188	[»]
4FA4	X-ray	2.14	C/E	58-188	[»]
4FA5	X-ray	1.94	C/E	58-188	[»]
4FA9	X-ray	2.09	C/E	58-188	[»]
4FAN	X-ray	2.08	C/E	58-188	[»]
4FAV	X-ray	2.08	C/E	58-188	[»]

ProteinModelPortal

P22619.

SMR

P22619. Positions 65-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6254N.

IntAct

P22619. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3910.

SABIO-RK

P22619.

UniPathway

UPA00895; UER00870.

Family and domain databases

Gene3D

2.60.30.10. 1 hit.

InterPro

IPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR004229. MeN_DH_Ltc.
[Graphical view]

Pfam

PF02975. Me-amine-dh_L. 1 hit.
[Graphical view]

PIRSF

PIRSF000192. Amine_dh_beta. 1 hit.

SUPFAM

SSF57561. MADH_Lt_C. 1 hit.

TIGRFAMs

TIGR02659. TTQ_MADH_Lt. 1 hit.

PROSITE

PS51318. TAT. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22619.

Entry information

Entry name

DHML_PARDE

Accession

Primary (citable) accession number: P22619

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program