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A1BB97

- A1BB97_PARDP

UniProt

A1BB97 - A1BB97_PARDP

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Protein
Submitted name: Methylamine dehydrogenase heavy chain
Gene
Pden_4730
Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei208 – 2081Acetate 2; via amide nitrogen
Metal bindingi284 – 2841SodiumImported
Metal bindingi287 – 2871SodiumImported
Metal bindingi289 – 2891Sodium; via carbonyl oxygenImported

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

Keywords - Ligandi

Metal-bindingImported, SodiumImported

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-4773-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Methylamine dehydrogenase heavy chainImported (EC:1.4.9.1Imported)
Gene namesi
Ordered Locus Names:Pden_4730Imported
Encoded oniPlasmid pPD1222
OrganismiParacoccus denitrificans (strain Pd 1222)Imported
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361: 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 PredictedImported
Add
BLAST
Chaini33 – 417385 PredictedImported
PRO_5000183176Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiA1BB97. 2 interactions.
STRINGi318586.Pden_4730.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliA1BB97.
SMRiA1BB97. Positions 36-417.

Miscellaneous databases

EvolutionaryTraceiA1BB97.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 694Acetate binding

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]
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.

A1BB97-1 [UniParc]FASTAAdd to Basket

« Hide

MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA    50
RAAAADLAAG QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG 100
RVIGMIDGGF LPNPVVADDG SFIAHASTVF SRIARGERTD YVEVFDPVTL 150
LPTADIELPD APRFLVGTYP WMTSLTPDGK TLLFYQFSPA PAVGVVDLEG 200
KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE GTPEITHTEV 250
FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 300
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRFVVVLDAK 350
TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS 400
VNQLGHGPQV ITTADMG 417
Length:417
Mass (Da):45,460
Last modified:January 23, 2007 - v1
Checksum:i819B4EEE2AC6D340
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000491 Genomic DNA. Translation: ABL72791.1.
RefSeqiYP_918487.1. NC_008688.1.

Genome annotation databases

EnsemblBacteriaiABL72791; ABL72791; Pden_4730.
GeneIDi4583233.
KEGGipde:Pden_4730.
PATRICi22860685. VBIParDen97112_4694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000491 Genomic DNA. Translation: ABL72791.1 .
RefSeqi YP_918487.1. NC_008688.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L4M X-ray 2.02 D/F 32-417 [» ]
3L4O X-ray 2.05 D/F 32-417 [» ]
3ORV X-ray 1.91 D/F 32-417 [» ]
3PXS X-ray 2.22 D/F 32-417 [» ]
3PXT X-ray 2.16 D/F 32-417 [» ]
3PXW X-ray 2.11 D/F 33-417 [» ]
3RLM X-ray 2.13 D/F 32-417 [» ]
3RMZ X-ray 1.72 D/F 32-417 [» ]
3RN0 X-ray 1.91 D/F 32-417 [» ]
3RN1 X-ray 1.93 D/F 32-417 [» ]
3SJL X-ray 1.63 D/F 32-417 [» ]
3SLE X-ray 2.52 D/F 33-417 [» ]
3SVW X-ray 1.86 D/F 32-417 [» ]
3SWS X-ray 1.86 D/F 32-417 [» ]
3SXT X-ray 1.81 D/F 32-417 [» ]
4FA1 X-ray 2.18 D/F 33-417 [» ]
4FA4 X-ray 2.14 D/F 33-417 [» ]
4FA5 X-ray 1.94 D/F 33-417 [» ]
4FA9 X-ray 2.09 D/F 33-417 [» ]
4FAN X-ray 2.08 D/F 33-417 [» ]
4FAV X-ray 2.08 D/F 33-417 [» ]
4FB1 X-ray 2.15 D/F 33-417 [» ]
4K3I X-ray 2.00 D/F 33-417 [» ]
4L1Q X-ray 1.92 D/F 33-417 [» ]
4L3G X-ray 2.05 D/F 33-417 [» ]
4L3H X-ray 1.79 D/F 33-417 [» ]
4O1Q X-ray 2.59 D/F 33-417 [» ]
ProteinModelPortali A1BB97.
SMRi A1BB97. Positions 36-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A1BB97. 2 interactions.
STRINGi 318586.Pden_4730.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL72791 ; ABL72791 ; Pden_4730 .
GeneIDi 4583233.
KEGGi pde:Pden_4730.
PATRICi 22860685. VBIParDen97112_4694.

Phylogenomic databases

eggNOGi NOG68563.
HOGENOMi HOG000147008.
KOi K15229.
OMAi DPGTQVW.
OrthoDBi EOG60W7QQ.

Enzyme and pathway databases

BioCyci PDEN318586:GCVQ-4773-MONOMER.

Miscellaneous databases

EvolutionaryTracei A1BB97.

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

« 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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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 IN COMPLEX WITH SODIUM.

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: September 3, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, PlasmidImported

External Data

Dasty 3

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