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Protein
Submitted name:

Methylamine dehydrogenase heavy chain

Gene

Pden_4730

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

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

OxidoreductaseImported

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-4773-MONOMER.
BRENDAi1.4.9.1. 3341.

Names & Taxonomyi

Protein namesi
Submitted name:
Methylamine dehydrogenase heavy chainImported (EC:1.4.9.1Imported)
Gene namesi
Ordered Locus Names:Pden_4730Imported
Encoded oniPlasmid pPD1222Imported
OrganismiParacoccus denitrificans (strain Pd 1222)Imported
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361 Componenti: Plasmid pPD1222

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 PotentialImportedAdd
BLAST
Chaini33 – 417385 PotentialImportedPRO_5000183176Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

IntActiA1BB97. 2 interactions.
STRINGi318586.Pden_4730.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4MX-ray2.02D/F32-417[»]
3L4OX-ray2.05D/F32-417[»]
3ORVX-ray1.91D/F32-417[»]
3PXSX-ray2.22D/F32-417[»]
3PXTX-ray2.16D/F32-417[»]
3PXWX-ray2.11D/F33-417[»]
3RLMX-ray2.13D/F32-417[»]
3RMZX-ray1.72D/F32-417[»]
3RN0X-ray1.91D/F32-417[»]
3RN1X-ray1.93D/F32-417[»]
3SJLX-ray1.63D/F32-417[»]
3SLEX-ray2.52D/F33-417[»]
3SVWX-ray1.86D/F32-417[»]
3SWSX-ray1.86D/F32-417[»]
3SXTX-ray1.81D/F32-417[»]
4FA1X-ray2.18D/F33-417[»]
4FA4X-ray2.14D/F33-417[»]
4FA5X-ray1.94D/F33-417[»]
4FA9X-ray2.09D/F33-417[»]
4FANX-ray2.08D/F33-417[»]
4FAVX-ray2.08D/F33-417[»]
4FB1X-ray2.15D/F33-417[»]
4K3IX-ray2.00D/F33-417[»]
4L1QX-ray1.92D/F33-417[»]
4L3GX-ray2.05D/F33-417[»]
4L3HX-ray1.79D/F33-417[»]
4O1QX-ray2.59D/F33-417[»]
SMRiA1BB97. Positions 36-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA1BB97.

Family & Domainsi

Keywords - Domaini

SignalImported

Phylogenomic databases

eggNOGiNOG68563.
HOGENOMiHOG000147008.
KOiK15229.
OMAiDPGTQVW.
OrthoDBiEOG60W7QQ.

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.

A1BB97-1 [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 SRFVVVLDAK
360 370 380 390 400
TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS
410
VNQLGHGPQV ITTADMG
Length:417
Mass (Da):45,460
Last modified:January 23, 2007 - v1
Checksum:i819B4EEE2AC6D340
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000491 Genomic DNA. Translation: ABL72791.1.
RefSeqiYP_918487.1. NC_008688.1.

Genome annotation databases

EnsemblBacteriaiABL72791; ABL72791; Pden_4730.
KEGGipde:Pden_4730.
PATRICi22860685. VBIParDen97112_4694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000491 Genomic DNA. Translation: ABL72791.1.
RefSeqiYP_918487.1. NC_008688.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4MX-ray2.02D/F32-417[»]
3L4OX-ray2.05D/F32-417[»]
3ORVX-ray1.91D/F32-417[»]
3PXSX-ray2.22D/F32-417[»]
3PXTX-ray2.16D/F32-417[»]
3PXWX-ray2.11D/F33-417[»]
3RLMX-ray2.13D/F32-417[»]
3RMZX-ray1.72D/F32-417[»]
3RN0X-ray1.91D/F32-417[»]
3RN1X-ray1.93D/F32-417[»]
3SJLX-ray1.63D/F32-417[»]
3SLEX-ray2.52D/F33-417[»]
3SVWX-ray1.86D/F32-417[»]
3SWSX-ray1.86D/F32-417[»]
3SXTX-ray1.81D/F32-417[»]
4FA1X-ray2.18D/F33-417[»]
4FA4X-ray2.14D/F33-417[»]
4FA5X-ray1.94D/F33-417[»]
4FA9X-ray2.09D/F33-417[»]
4FANX-ray2.08D/F33-417[»]
4FAVX-ray2.08D/F33-417[»]
4FB1X-ray2.15D/F33-417[»]
4K3IX-ray2.00D/F33-417[»]
4L1QX-ray1.92D/F33-417[»]
4L3GX-ray2.05D/F33-417[»]
4L3HX-ray1.79D/F33-417[»]
4O1QX-ray2.59D/F33-417[»]
SMRiA1BB97. Positions 36-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiA1BB97. 2 interactions.
STRINGi318586.Pden_4730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL72791; ABL72791; Pden_4730.
KEGGipde:Pden_4730.
PATRICi22860685. VBIParDen97112_4694.

Phylogenomic databases

eggNOGiNOG68563.
HOGENOMiHOG000147008.
KOiK15229.
OMAiDPGTQVW.
OrthoDBiEOG60W7QQ.

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-4773-MONOMER.
BRENDAi1.4.9.1. 3341.

Miscellaneous databases

EvolutionaryTraceiA1BB97.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine ."
    Abu Tarboush N., Jensen L.M., Feng M., Tachikawa H., Wilmot C.M., Davidson V.L.
    Biochemistry 49:9783-9791(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 32-417, ACTIVE SITE.
  3. "In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex."
    Jensen L.M., Sanishvili R., Davidson V.L., Wilmot C.M.
    Science 327:1392-1394(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 32-417, ACTIVE SITE.
  4. "Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation."
    Yukl E.T., Goblirsch B.R., Davidson V.L., Wilmot C.M.
    Biochemistry 50:2931-2938(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 33-417, ACTIVE SITE.
  5. "Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis."
    Tarboush N.A., Jensen L.M., Yukl E.T., Geng J., Liu A., Wilmot C.M., Davidson V.L.
    Proc. Natl. Acad. Sci. U.S.A. 108:16956-16961(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 32-417, ACTIVE SITE.
  6. "Mutagenesis of tryptophan199 reveals that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis."
    Jensen L.M.R., Wilmot C.M.
    Submitted (APR-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 32-417, ACTIVE SITE.
  7. "Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG."
    Jensen L.M.R., Wilmot C.M.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-417, ACTIVE SITE.
  8. "Crystal Structure of the Quinone Form of Methylamine Dehydrogenase in Complex with the Diferric Form of MauG."
    Jensen L.M.R., Wilmot C.M.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 32-417, ACTIVE SITE.
  9. "Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG."
    Feng M., Jensen L.M., Yukl E.T., Wei X., Liu A., Wilmot C.M., Davidson V.L.
    Biochemistry 51:1598-1606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 32-417, ACTIVE SITE.
  10. "Structures of MauG in complex with quinol and quinone MADH."
    Yukl E.T., Jensen L.M., Davidson V.L., Wilmot C.M.
    Acta Crystallogr. F 69:738-743(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-417, ACTIVE SITE.
  11. "Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG."
    Abu Tarboush N., Yukl E.T., Shin S., Feng M., Wilmot C.M., Davidson V.L.
    Biochemistry 52:6358-6367(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 33-417, ACTIVE SITE.
  12. "Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis."
    Yukl E.T., Liu F., Krzystek J., Shin S., Jensen L.M., Davidson V.L., Wilmot C.M., Liu A.
    Proc. Natl. Acad. Sci. U.S.A. 110:4569-4573(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 33-417, ACTIVE SITE.
  13. "Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG."
    Shin S., Yukl E.T., Sehanobish E., Wilmot C.M., Davidson V.L.
    Biochemistry 53:1342-1349(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 33-417, ACTIVE SITE.

Entry informationi

Entry nameiA1BB97_PARDP
AccessioniPrimary (citable) accession number: A1BB97
Entry historyi
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, PlasmidImported, Reference proteomeImported

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.