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Protein

Methylamine dehydrogenase light chain

Gene

mauA

Organism
Paracoccus versutus (Thiobacillus versutus)
Status
Reviewed-Annotation score: 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 + 2 oxidized [amicyanin] = formaldehyde + NH3 + 2 reduced [amicyanin].

Cofactori

tryptophan tryptophylquinone residueNote: Uses a protein-derived tryptophan tryptophylquinone (TTQ) cofactor.

Pathwayi: methylamine degradation

This protein is involved in step 1 of the subpathway that synthesizes formaldehyde from methylamine.
Proteins known to be involved in this subpathway in this organism are:
  1. Methylamine dehydrogenase light chain (mauA)
This subpathway is part of the pathway methylamine degradation, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formaldehyde from methylamine, the pathway methylamine degradation and in One-carbon metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3902.
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)
Methylamine dehydrogenase subunit beta
Gene namesi
Name:mauA
Synonyms:madB
OrganismiParacoccus versutus (Thiobacillus versutus)
Taxonomic identifieri34007 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5757Tat-type signal2 PublicationsAdd
BLAST
Chaini58 – 188131Methylamine dehydrogenase light chainPRO_0000025576Add
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)
Modified residuei114 – 1141Tryptophylquinone
Disulfide bondi135 ↔ 166

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has 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.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 753Combined sources
Helixi83 – 853Combined sources
Beta strandi89 – 924Combined sources
Helixi93 – 953Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi114 – 1207Combined sources
Turni121 – 1244Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi142 – 1465Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 1633Combined sources
Helixi170 – 1723Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi183 – 1864Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MAEX-ray2.80L64-187[»]
1MAFX-ray2.60L64-187[»]
2MADX-ray2.25L64-187[»]
3C75X-ray2.50L/M1-188[»]
ProteinModelPortaliP22641.
SMRiP22641. Positions 64-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22641.

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.

P22641-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGNFRFDDM VEKLSRRVAG RTSRRGAIGR LGTVLAGAAL VPLLPVDRRG
60 70 80 90 100
RVSRANAAGP AEGVDPRAKW QPQDNDIQAC DYWRHCSIDG NICDCSGGSL
110 120 130 140 150
TNCPPGTKLA TASWVASCYN PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG
160 170 180
ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI SPIVGKAS
Length:188
Mass (Da):20,358
Last modified:November 1, 1997 - v2
Checksum:i923C5461737C63FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891D → A AA sequence (PubMed:2792083).Curated
Sequence conflicti97 – 971G → A AA sequence (PubMed:2792083).Curated
Sequence conflicti102 – 1021N → S AA sequence (PubMed:2792083).Curated
Sequence conflicti108 – 1125KLATA → LVASG AA sequence (PubMed:2792083).Curated
Sequence conflicti116 – 1161A → G AA sequence (PubMed:2792083).Curated
Sequence conflicti122 – 1298TDGQSYLI → PDPNKYIT AA sequence (PubMed:2792083).Curated
Sequence conflicti144 – 1441P → A AA sequence (PubMed:2792083).Curated
Sequence conflicti156 – 1594RPEF → NKD AA sequence (PubMed:2792083).Curated
Sequence conflicti169 – 1691A → G AA sequence (PubMed:2792083).Curated
Sequence conflicti172 – 1732DA → G AA sequence (PubMed:2792083).Curated
Sequence conflicti179 – 1791T → S AA sequence (PubMed:2792083).Curated
Sequence conflicti183 – 1886IVGKAS → VSGA AA sequence (PubMed:2792083).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58001 Genomic DNA. Translation: AAA50570.1.
PIRiS19731.
RefSeqiWP_036750427.1. NZ_JRKO01000005.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58001 Genomic DNA. Translation: AAA50570.1.
PIRiS19731.
RefSeqiWP_036750427.1. NZ_JRKO01000005.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MAEX-ray2.80L64-187[»]
1MAFX-ray2.60L64-187[»]
2MADX-ray2.25L64-187[»]
3C75X-ray2.50L/M1-188[»]
ProteinModelPortaliP22641.
SMRiP22641. Positions 64-187.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00895; UER00870.
BioCyciMetaCyc:MONOMER-3902.

Miscellaneous databases

EvolutionaryTraceiP22641.

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.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus."
    Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F., Beintema J.J., Duine J.A., Canters G.W.
    Eur. J. Biochem. 202:1003-1012(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure of quinoprotein methylamine dehydrogenase at 2.25-A resolution."
    Vellieux F.M.D., Huitema F., Groendijk H., Kalk K.H., Jzn J.F., Jongejan J.A., Duine J.A., Petratos K., Drenth J., Hol W.G.J.
    EMBO J. 8:2171-2178(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-188, X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  3. "N-terminal heterogeneity of methylamine dehydrogenase from Thiobacillus versutus."
    Van Beeumen J., Van Driessche G., Huitema F., Duine J.A., Canters G.W.
    FEBS Lett. 333:188-192(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-66.
  4. "Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus."
    Vellieux F.M.D., Kalk K.H., Hol W.G.J.
    Acta Crystallogr. B 46:806-823(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Entry informationi

Entry nameiDHML_PARVE
AccessioniPrimary (citable) accession number: P22641
Secondary accession number(s): Q56458
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: March 16, 2016
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, Direct protein sequencing

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.