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P23006

- DHMH_PARVE

UniProt

P23006 - DHMH_PARVE

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Protein
Methylamine dehydrogenase heavy chain
Gene
mauB, madA
Organism
Paracoccus versutus (Thiobacillus versutus)
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-3901.

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
Synonyms:madA
OrganismiParacoccus versutus (Thiobacillus versutus)
Taxonomic identifieri34007 [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 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 426395Methylamine dehydrogenase heavy chain
PRO_0000025581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi221 ↔ 236

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Tetramer of two light and two heavy chains.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 6714
Beta strandi86 – 916
Turni93 – 953
Beta strandi97 – 1059
Turni106 – 1083
Beta strandi111 – 1177
Beta strandi122 – 1254
Beta strandi132 – 14110
Beta strandi144 – 15411
Turni156 – 1583
Beta strandi161 – 1677
Helixi179 – 1813
Beta strandi182 – 1843
Beta strandi188 – 1958
Beta strandi197 – 1993
Beta strandi201 – 2066
Turni207 – 2104
Beta strandi211 – 2177
Beta strandi220 – 2289
Beta strandi231 – 2366
Beta strandi239 – 2457
Beta strandi252 – 2554
Turni274 – 2763
Beta strandi278 – 2836
Beta strandi286 – 2938
Beta strandi298 – 3003
Beta strandi304 – 3074
Turni309 – 3113
Helixi312 – 3143
Beta strandi316 – 3183
Beta strandi320 – 3223
Beta strandi324 – 3274
Turni328 – 3314
Beta strandi332 – 3398
Beta strandi349 – 3568
Turni357 – 3593
Beta strandi362 – 37211
Beta strandi374 – 3774
Beta strandi380 – 3823
Beta strandi384 – 3896
Turni390 – 3934
Beta strandi394 – 3996
Turni400 – 4023
Beta strandi405 – 4095
Beta strandi413 – 4153
Beta strandi418 – 4203

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MAEX-ray2.80H59-400[»]
1MAFX-ray2.60H59-400[»]
2MADX-ray2.25H59-400[»]
3C75X-ray2.50H/J1-426[»]
ProteinModelPortaliP23006.
SMRiP23006. Positions 72-424.

Miscellaneous databases

EvolutionaryTraceiP23006.

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.

P23006-1 [UniParc]FASTAAdd to Basket

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MASARESTPR YLTLIGATLA CSALALGAAQ AQTEPAEPEA PAETAAADAA    50
GQTEGQRGAA EAAAALAAGE ADEPVILEAP APDARRVYIQ DPAHFAAITQ 100
QFVIDGSTGR ILGMTDGGFL PHPVAAEDGS FFAQASTVFE RIARGKRTDY 150
VEVFDPVTFL PIADIELPDA PRFLVGTYQW MNALTPDNKN LLFYQFSPAP 200
AVGVVDLEGK TFDRMLDVPD CYHIFPASPT VFYMNCRDGS LARVDFADGE 250
TKVTNTEVFH TEDELLINHP AFSLRSGRLV WPTYTGKIFQ ADLTAEGATF 300
RAPIEALTEA ERADDWRPGG WQQTAYHRQS DRIYLLVDQR DEWKHKAASR 350
FVVVLNAETG ERINKIELGH EIDSINVSQD AEPLLYALSA GTQTLHIYDA 400
ATGEELRSVD QLGRGPQIIT THDMDS 426
Length:426
Mass (Da):46,388
Last modified:November 1, 1997 - v2
Checksum:i4ECDF8F6A7AE8696
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08575 Genomic DNA. Translation: AAA72335.1.
PIRiA36934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08575 Genomic DNA. Translation: AAA72335.1 .
PIRi A36934.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MAE X-ray 2.80 H 59-400 [» ]
1MAF X-ray 2.60 H 59-400 [» ]
2MAD X-ray 2.25 H 59-400 [» ]
3C75 X-ray 2.50 H/J 1-426 [» ]
ProteinModelPortali P23006.
SMRi P23006. Positions 72-424.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3901.

Miscellaneous databases

EvolutionaryTracei P23006.

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. "Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus."
    Huitema F., van Beeumen J., van Driessche G., Duine J.A., Canters G.W.
    J. Bacteriol. 175:6254-6259(1993) [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: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
  3. "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 nameiDHMH_PARVE
AccessioniPrimary (citable) accession number: P23006
Secondary accession number(s): Q60052
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: October 16, 2013
This is version 85 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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