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P22619

- DHML_PARDE

UniProt

P22619 - DHML_PARDE

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Protein

Methylamine dehydrogenase light chain

Gene
mauA
Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.

Catalytic activityi

Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin.

Cofactori

Contains 1 tryptophan tryptophylquinone per subunit.

Pathwayi

GO - Molecular functioni

  1. amine dehydrogenase activity Source: InterPro
  2. methylamine dehydrogenase (amicyanin) activity Source: UniProtKB-EC

GO - Biological processi

  1. amine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3910.
SABIO-RKP22619.
UniPathwayiUPA00895; UER00870.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylamine dehydrogenase light chain (EC:1.4.9.1)
Short name:
MADH
Alternative name(s):
Methylamine dehydrogenase (amicyanin)
Gene namesi
Name:mauA
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5757Tat-type signal Reviewed predictionAdd
BLAST
Chaini58 – 188131Methylamine dehydrogenase light chainPRO_0000025575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi80 ↔ 145
Disulfide bondi86 ↔ 118
Disulfide bondi93 ↔ 178
Disulfide bondi95 ↔ 143
Disulfide bondi103 ↔ 134
Cross-linki114 ↔ 165Tryptophan tryptophylquinone (Trp-Trp)1 Publication
Modified residuei114 – 1141Tryptophylquinone1 Publication
Disulfide bondi135 ↔ 166

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, TTQ

Interactioni

Subunit structurei

Heterotetramer of two light and two heavy chains.

Protein-protein interaction databases

DIPiDIP-6254N.
IntActiP22619. 1 interaction.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 683
Beta strandi73 – 753
Helixi83 – 853
Beta strandi89 – 924
Helixi93 – 964
Beta strandi100 – 1034
Beta strandi114 – 1207
Turni121 – 1244
Beta strandi125 – 13713
Beta strandi142 – 1465
Helixi157 – 1593
Beta strandi161 – 1633
Helixi170 – 1723
Beta strandi175 – 1806
Beta strandi183 – 1853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25B/F/J/N58-188[»]
1MG3X-ray2.40B/F/J/N58-188[»]
2BBKX-ray1.75L/M64-188[»]
2GC4X-ray1.90B/F/J/N58-188[»]
2GC7X-ray1.90B/F/J/N58-188[»]
2J55X-ray2.15L/M58-188[»]
2J56X-ray2.10L/M58-188[»]
2J57X-ray2.25K/L/M/N58-188[»]
2MTAX-ray2.40L64-188[»]
3ORVX-ray1.91C/E58-188[»]
3PXSX-ray2.22C/E58-188[»]
3PXTX-ray2.16C/E58-188[»]
3PXWX-ray2.11C/E58-188[»]
3RLMX-ray2.13C/E58-188[»]
3RMZX-ray1.72C/E58-188[»]
3RN0X-ray1.91C/E58-188[»]
4FA1X-ray2.18C/E58-188[»]
4FA4X-ray2.14C/E58-188[»]
4FA5X-ray1.94C/E58-188[»]
4FA9X-ray2.09C/E58-188[»]
4FANX-ray2.08C/E58-188[»]
4FAVX-ray2.08C/E58-188[»]
4FB1X-ray2.15C/E58-188[»]
4K3IX-ray2.00C/E58-188[»]
ProteinModelPortaliP22619.
SMRiP22619. Positions 65-187.

Miscellaneous databases

EvolutionaryTraceiP22619.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.30.10. 1 hit.
InterProiIPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR004229. MeN_DH_Ltc.
[Graphical view]
PfamiPF02975. Me-amine-dh_L. 1 hit.
[Graphical view]
PIRSFiPIRSF000192. Amine_dh_beta. 1 hit.
SUPFAMiSSF57561. SSF57561. 1 hit.
TIGRFAMsiTIGR02659. TTQ_MADH_Lt. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22619-1 [UniParc]FASTAAdd to Basket

« Hide

MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG    50
RVSRANAADA PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL 100
TNCPPGTKLA TASWVASCYN PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG 150
ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI SPIVGKAS 188
Length:188
Mass (Da):20,393
Last modified:April 1, 1993 - v2
Checksum:iE3D9DE4454268BE8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90098 Genomic DNA. Translation: AAA25578.1.
X55665 Genomic DNA. Translation: CAA39198.1.
PIRiJH0661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90098 Genomic DNA. Translation: AAA25578.1 .
X55665 Genomic DNA. Translation: CAA39198.1 .
PIRi JH0661.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4FB1 X-ray 2.15 C/E 58-188 [» ]
4K3I X-ray 2.00 C/E 58-188 [» ]
ProteinModelPortali P22619.
SMRi P22619. Positions 65-187.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6254N.
IntActi P22619. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00895 ; UER00870 .
BioCyci MetaCyc:MONOMER-3910.
SABIO-RK P22619.

Miscellaneous databases

EvolutionaryTracei P22619.

Family and domain databases

Gene3Di 2.60.30.10. 1 hit.
InterProi IPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR004229. MeN_DH_Ltc.
[Graphical view ]
Pfami PF02975. Me-amine-dh_L. 1 hit.
[Graphical view ]
PIRSFi PIRSF000192. Amine_dh_beta. 1 hit.
SUPFAMi SSF57561. SSF57561. 1 hit.
TIGRFAMsi TIGR02659. TTQ_MADH_Lt. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiDHML_PARDE
AccessioniPrimary (citable) accession number: P22619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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