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A1BB97 (A1BB97_PARDP) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
EC=1.4.9.1 EMBL ABL72791.1
Gene names
Ordered Locus Names:Pden_4730 EMBL ABL72791.1
Encoded onPlasmid pPD1222
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP] EMBL ABL72791.1
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential EMBL ABL72791.1
Chain33 – 417385 Potential EMBL ABL72791.1
PRO_5000183176

Regions

Region66 – 694Acetate 1 binding PDB 3L4O PDB 3L4M PDB 3PXT PDB 3PXS PDB 3RLM PDB 3RMZ PDB 3RN1 PDB 3SLE PDB 3SVW PDB 4FA1 PDB 4FA4 PDB 4FA9 PDB 4L3G
Region66 – 694Acetate binding

Sites

Metal binding2841Sodium PDB 4O1Q
Metal binding2871Sodium PDB 4O1Q
Metal binding2891Sodium; via carbonyl oxygen PDB 4O1Q
Binding site2081Acetate 2; via amide nitrogen

Sequences

Sequence LengthMass (Da)Tools
A1BB97 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 819B4EEE2AC6D340

FASTA41745,460
        10         20         30         40         50         60 
MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA RAAAADLAAG 

        70         80         90        100        110        120 
QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG RVIGMIDGGF LPNPVVADDG 

       130        140        150        160        170        180 
SFIAHASTVF SRIARGERTD YVEVFDPVTL LPTADIELPD APRFLVGTYP WMTSLTPDGK 

       190        200        210        220        230        240 
TLLFYQFSPA PAVGVVDLEG KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE 

       250        260        270        280        290        300 
GTPEITHTEV FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 

       310        320        330        340        350        360 
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRFVVVLDAK TGERLAKFEM 

       370        380        390        400        410 
GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS VNQLGHGPQV ITTADMG 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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 IN COMPLEX WITH ACETATE.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000491 Genomic DNA. Translation: ABL72791.1.
RefSeqYP_918487.1. NC_008688.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalA1BB97.
SMRA1BB97. Positions 36-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA1BB97. 2 interactions.
STRING318586.Pden_4730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL72791; ABL72791; Pden_4730.
GeneID4583233.
KEGGpde:Pden_4730.
PATRIC22860685. VBIParDen97112_4694.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG68563.
HOGENOMHOG000147008.
KOK15229.
OMADPGTQVW.
OrthoDBEOG60W7QQ.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-4773-MONOMER.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR013476. MeN_DH_Hvc.
IPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
PIRSFPIRSF017797. TTQ_MADH_Hv. 1 hit.
SUPFAMSSF50969. SSF50969. 1 hit.
TIGRFAMsTIGR02658. TTQ_MADH_Hv. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceA1BB97.

Entry information

Entry nameA1BB97_PARDP
AccessionPrimary (citable) accession number: A1BB97
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)