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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 + 2 oxidized [amicyanin] = formaldehyde + NH3 + 2 reduced [amicyanin].

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-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

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Or 26Sequence analysisAdd BLAST28
ChainiPRO_000002558029 – 417Methylamine dehydrogenase heavy chainAdd BLAST389

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 58Combined sources19
Beta strandi77 – 82Combined sources6
Helixi84 – 86Combined sources3
Beta strandi88 – 96Combined sources9
Turni97 – 100Combined sources4
Beta strandi101 – 108Combined sources8
Beta strandi113 – 116Combined sources4
Beta strandi123 – 132Combined sources10
Beta strandi135 – 145Combined sources11
Turni147 – 149Combined sources3
Beta strandi152 – 158Combined sources7
Helixi170 – 172Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi179 – 186Combined sources8
Beta strandi188 – 190Combined sources3
Beta strandi192 – 197Combined sources6
Turni198 – 201Combined sources4
Beta strandi202 – 208Combined sources7
Beta strandi211 – 219Combined sources9
Beta strandi222 – 227Combined sources6
Beta strandi232 – 236Combined sources5
Beta strandi239 – 241Combined sources3
Beta strandi244 – 247Combined sources4
Beta strandi263 – 265Combined sources3
Turni266 – 269Combined sources4
Beta strandi270 – 275Combined sources6
Beta strandi278 – 284Combined sources7
Beta strandi296 – 299Combined sources4
Helixi301 – 305Combined sources5
Beta strandi308 – 310Combined sources3
Beta strandi312 – 314Combined sources3
Beta strandi316 – 319Combined sources4
Turni320 – 323Combined sources4
Beta strandi324 – 331Combined sources8
Beta strandi341 – 348Combined sources8
Turni349 – 351Combined sources3
Beta strandi354 – 364Combined sources11
Beta strandi366 – 369Combined sources4
Beta strandi372 – 374Combined sources3
Beta strandi376 – 381Combined sources6
Turni382 – 385Combined sources4
Beta strandi386 – 391Combined sources6
Turni392 – 394Combined sources3
Beta strandi397 – 401Combined sources5
Beta strandi410 – 412Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6253N.
IntActiP29894. 1 interactor.

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...

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: November 2, 2016
This is version 101 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

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.