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P29894

- DHMH_PARDE

UniProt

P29894 - DHMH_PARDE

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Protein

Methylamine dehydrogenase heavy chain

Gene

mauB

Organism
Paracoccus denitrificans
Status
Reviewed - 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-KW
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 – 5819
Beta strandi77 – 826
Helixi84 – 863
Beta strandi88 – 969
Turni97 – 1004
Beta strandi101 – 1088
Beta strandi113 – 1164
Beta strandi123 – 13210
Beta strandi135 – 14511
Turni147 – 1493
Beta strandi152 – 1587
Helixi170 – 1723
Beta strandi173 – 1753
Beta strandi179 – 1868
Beta strandi188 – 1903
Beta strandi192 – 1976
Turni198 – 2014
Beta strandi202 – 2087
Beta strandi211 – 2199
Beta strandi222 – 2276
Beta strandi232 – 2365
Beta strandi239 – 2413
Beta strandi244 – 2474
Beta strandi263 – 2653
Turni266 – 2694
Beta strandi270 – 2756
Beta strandi278 – 2847
Beta strandi296 – 2994
Helixi301 – 3055
Beta strandi308 – 3103
Beta strandi312 – 3143
Beta strandi316 – 3194
Turni320 – 3234
Beta strandi324 – 3318
Beta strandi341 – 3488
Turni349 – 3513
Beta strandi354 – 36411
Beta strandi366 – 3694
Beta strandi372 – 3743
Beta strandi376 – 3816
Turni382 – 3854
Beta strandi386 – 3916
Turni392 – 3943
Beta strandi397 – 4015
Beta strandi410 – 4123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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]
PIRSFiPIRSF017797. TTQ_MADH_Hv. 1 hit.
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:
EMBL
GenBank
DDBJ
Links Updated
M90099 Genomic DNA. Translation: AAA25580.1.
U12464 Genomic DNA. Translation: AAA56724.1.
PIRiJH0660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90099 Genomic DNA. Translation: AAA25580.1 .
U12464 Genomic DNA. Translation: AAA56724.1 .
PIRi JH0660.

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 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 [» ]
ProteinModelPortali P29894.
SMRi P29894. Positions 36-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6253N.
IntActi P29894. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3909.
SABIO-RK P29894.

Miscellaneous databases

EvolutionaryTracei P29894.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
Pfami PF06433. Me-amine-dh_H. 1 hit.
[Graphical view ]
PIRSFi PIRSF017797. TTQ_MADH_Hv. 1 hit.
SUPFAMi SSF50969. SSF50969. 1 hit.
TIGRFAMsi TIGR02658. TTQ_MADH_Hv. 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. "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).

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: October 29, 2014
This is version 93 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