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Protein

Methylamine dehydrogenase heavy chain

Gene

mauB

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: Annotation score: 4 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.

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3909.
SABIO-RKP29894.

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Or 26Sequence AnalysisAdd
BLAST
Chaini29 – 417389Methylamine dehydrogenase heavy chainPRO_0000025580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi212 ↔ 227

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Tetramer of two light and two heavy chains.1 Publication

Protein-protein interaction databases

DIPiDIP-6253N.
IntActiP29894. 1 interaction.

Structurei

Secondary structure

1
417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5819Combined sources
Beta strandi77 – 826Combined sources
Helixi84 – 863Combined sources
Beta strandi88 – 969Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi135 – 14511Combined sources
Turni147 – 1493Combined sources
Beta strandi152 – 1587Combined sources
Helixi170 – 1723Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 1976Combined sources
Turni198 – 2014Combined sources
Beta strandi202 – 2087Combined sources
Beta strandi211 – 2199Combined sources
Beta strandi222 – 2276Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi263 – 2653Combined sources
Turni266 – 2694Combined sources
Beta strandi270 – 2756Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi296 – 2994Combined sources
Helixi301 – 3055Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi316 – 3194Combined sources
Turni320 – 3234Combined sources
Beta strandi324 – 3318Combined sources
Beta strandi341 – 3488Combined sources
Turni349 – 3513Combined sources
Beta strandi354 – 36411Combined sources
Beta strandi366 – 3694Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi376 – 3816Combined sources
Turni382 – 3854Combined sources
Beta strandi386 – 3916Combined sources
Turni392 – 3943Combined sources
Beta strandi397 – 4015Combined sources
Beta strandi410 – 4123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25A/E/I/M28-417[»]
1MG3X-ray2.40A/E/I/M28-417[»]
2BBKX-ray1.75H/J63-417[»]
2GC4X-ray1.90A/E/I/M32-417[»]
2GC7X-ray1.90A/E/I/M32-417[»]
2J55X-ray2.15H/J32-417[»]
2J56X-ray2.10H/J32-417[»]
2J57X-ray2.25G/H/I/J32-417[»]
2MTAX-ray2.40H45-417[»]
ProteinModelPortaliP29894.
SMRiP29894. Positions 36-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29894.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 1 hit.
TIGRFAMsiTIGR02658. TTQ_MADH_Hv. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P29894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA
60 70 80 90 100
RAAAADLAAG QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG
110 120 130 140 150
RVIGMIDGGF LPNPVVADDG SFIAHASTVF SRIARGERTD YVEVFDPVTL
160 170 180 190 200
LPTADIELPD APRFLVGTYP WMTSLTPDGK TLLFYQFSPA PAVGVVDLEG
210 220 230 240 250
KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE GTPEITHTEV
260 270 280 290 300
FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT
310 320 330 340 350
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK
360 370 380 390 400
TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS
410
VNQLGHGPQV ITTADMG
Length:417
Mass (Da):45,440
Last modified:April 1, 1993 - v1
Checksum:i8187A8B694208BE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90099 Genomic DNA. Translation: AAA25580.1.
U12464 Genomic DNA. Translation: AAA56724.1.
PIRiJH0660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90099 Genomic DNA. Translation: AAA25580.1.
U12464 Genomic DNA. Translation: AAA56724.1.
PIRiJH0660.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25A/E/I/M28-417[»]
1MG3X-ray2.40A/E/I/M28-417[»]
2BBKX-ray1.75H/J63-417[»]
2GC4X-ray1.90A/E/I/M32-417[»]
2GC7X-ray1.90A/E/I/M32-417[»]
2J55X-ray2.15H/J32-417[»]
2J56X-ray2.10H/J32-417[»]
2J57X-ray2.25G/H/I/J32-417[»]
2MTAX-ray2.40H45-417[»]
ProteinModelPortaliP29894.
SMRiP29894. Positions 36-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6253N.
IntActiP29894. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3909.
SABIO-RKP29894.

Miscellaneous databases

EvolutionaryTraceiP29894.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 1 hit.
TIGRFAMsiTIGR02658. TTQ_MADH_Hv. 1 hit.
ProtoNetiSearch...

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(1991) [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(1993) [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(1991) [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(1991) [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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiDHMH_PARDE
AccessioniPrimary (citable) accession number: P29894
Secondary accession number(s): Q79D76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 1, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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 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.