Conserved Protein Domain Family
MauD

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TIGR02661: MauD 
methylamine dehydrogenase accessory protein MauD
This protein, MauD, appears critical to proper formation of the small subunit of methylamine dehydrogenase, which has both an unusual tryptophan tryptophylquinone cofactor and multiple disulfide bonds. MauD shares sequence similarity, including a CPxC motif, with a number of thiol:disulfide interchange proteins. In MauD mutants, the small subunit apparently does not form properly and is rapidly degraded. [Protein fate, Protein folding and stabilization, Energy metabolism, Amino acids and amines]
Statistics
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PSSM-Id: 131709
View PSSM: TIGR02661
Aligned: 3 rows
Threshold Bit Score: 331.054
Threshold Setting Gi: 2497800
Created: 8-Oct-2014
Updated: 2-Oct-2020
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Q49126   5 FLIASNVLLWLALIGCAVLMLGLLRQVGLLHERSSPMGAMITDHGPDVGDAAPTFDLPDHSGAMVRIGGPSALKRPTLLM 84  Methylobacterium exto...
P29895   4 FLIASNILLWLAFLGVTVVMLGLMRQVGLLHERSSPMGAMITDHGPDIGDAAPEFELPDFFGRPVRIGGAEAQGRQTLLM 83  Paracoccus denitrificans
Q50232   5 ILIASNVLLWGAFLALAALMLGVIRQIGLLHERSAPLGAMMIDHGPDVGERSPIFNVNTFDGEPVLVGRSITPGRPSLLM 84  Methylophilus methylo...
Q49126  85 FTAPTCPVCDKLFPLIKSIARAEKFSVVMISDGQPDEHQRFLAKHELGDIRYVVSAEVGMAFQVGKIPYGVLLDPEGVIR 164 Methylobacterium exto...
P29895  84 FTAPSCPVCDKLFPIIKSIGRAEGINVVMISDGAPEEHRRFLDSHELGEMRYVVSAEAGMAFQVGKIPYGVLLDGQGIIR 163 Paracoccus denitrificans
Q50232  85 FTGPSCPICQKLLPIIRSVAAIEETDVILISDGTQAEHRQFLKDHPLDGELYVVSAEIGMRYQVSKVPYGVLLDQDGKIL 164 Methylophilus methylo...
Q49126 165 AKGLTNTREHLESLLEADKSGFASIQQFM 193 Methylobacterium extorquens AM1
P29895 164 AKGLTNTREHLESLLEADRTGFASLQQYM 192 Paracoccus denitrificans
Q50232 165 AKGLCNTREHVESLFETIREGHSTLQNYL 193 Methylophilus methylotrophus
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