Methylamine dehydrogenase heavy chain precursor

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P29894 (DHMH_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
Methylamine dehydrogenase (amicyanin)

Gene names

Name:

mauB

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	417 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.
Subunit structure	Tetramer of two light and two heavy chains.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the aromatic amine dehydrogenase heavy chain family.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW methylamine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 28

Or 26 Potential

Chain

29 – 417

389

Methylamine dehydrogenase heavy chain

PRO_0000025580

Amino acid modifications

Disulfide bond

212 ↔ 227

Secondary structure

417

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29894 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 8187A8B694208BE2
Show »

FASTA

417

45,440

        10         20         30         40         50         60 
MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA RAAAADLAAG 

        70         80         90        100        110        120 
QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG RVIGMIDGGF LPNPVVADDG 

       130        140        150        160        170        180 
SFIAHASTVF SRIARGERTD YVEVFDPVTL LPTADIELPD APRFLVGTYP WMTSLTPDGK 

       190        200        210        220        230        240 
TLLFYQFSPA PAVGVVDLEG KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE 

       250        260        270        280        290        300 
GTPEITHTEV FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 

       310        320        330        340        350        360 
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK TGERLAKFEM 

       370        380        390        400        410 
GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS VNQLGHGPQV ITTADMG

« Hide

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]	"Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator." van Spanning R.J.M., van der Palen C.J., Slotboom D.J., Reijnders W.N., Stouthamer A.H., Duine J.A. Eur. J. Biochem. 226:201-210(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69. Strain: ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627.
[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).
[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) 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

M90099 Genomic DNA. Translation: AAA25580.1.
U12464 Genomic DNA. Translation: AAA56724.1.

PIR

JH0660.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MG2	X-ray	2.25	A/E/I/M	28-417	[»]
1MG3	X-ray	2.40	A/E/I/M	28-417	[»]
2BBK	X-ray	1.75	H/J	63-417	[»]
2GC4	X-ray	1.90	A/E/I/M	32-417	[»]
2GC7	X-ray	1.90	A/E/I/M	32-417	[»]
2J55	X-ray	2.15	H/J	32-417	[»]
2J56	X-ray	2.10	H/J	32-417	[»]
2J57	X-ray	2.25	G/H/I/J	32-417	[»]
2MTA	X-ray	2.40	H	45-417	[»]

ProteinModelPortal

P29894.

SMR

P29894. Positions 36-417.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6253N.

IntAct

P29894. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3909.

SABIO-RK

P29894.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

Pfam

PF06433. Me-amine-dh_H. 1 hit.
[Graphical view]

PIRSF

PIRSF017797. TTQ_MADH_Hv. 1 hit.

SUPFAM

SSF50969. Amine_DH_B_like. 1 hit.

TIGRFAMs

TIGR02658. TTQ_MADH_Hv. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P29894.

Entry information

Entry name

DHMH_PARDE

Accession

Primary (citable) accession number: P29894
Secondary accession number(s): Q79D76

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents