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Protein
Submitted name:

2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase

Gene

mlr6788

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei106 – 1061FADCombined sources
Binding sitei130 – 1301FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei156 – 1561FAD; via carbonyl oxygenCombined sources
Binding sitei181 – 1811FADCombined sources
Binding sitei288 – 2881FADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 222FADCombined sources
Nucleotide bindingi41 – 422FADCombined sources
Nucleotide bindingi295 – 3028FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-5382-MONOMER.
BRENDAi1.14.12.4. 3243.

Names & Taxonomyi

Protein namesi
Submitted name:
2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenaseImported
Gene namesi
Ordered Locus Names:mlr6788Imported
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)Imported
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
ProteomesiUP000000552 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi266835.mlr6788.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ALJX-ray1.48A1-379[»]
3ALLX-ray1.78A/B1-379[»]
3ALMX-ray1.77A/B1-379[»]
3GMBX-ray2.10A/B1-379[»]
3GMCX-ray2.10A/B1-379[»]
4GF7X-ray1.58A1-379[»]
4H2NX-ray2.30A1-379[»]
4H2PX-ray1.98A/B/C/D1-379[»]
4H2QX-ray1.50A1-379[»]
4H2RX-ray2.47A/B1-379[»]
4JY2X-ray1.94A/B1-379[»]
4JY3X-ray1.77A/B1-379[»]
ProteinModelPortaliQ988D3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ988D3.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000000640.
KOiK18071.
OMAiCNENELY.
OrthoDBiEOG6J48MG.

Family and domain databases

InterProiIPR002938. mOase_FAD-bd.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q988D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVNKTPGK TRRAEVAGGG FAGLTAAIAL KQNGWDVRLH EKSSELRAFG
60 70 80 90 100
AGIYLWHNGL RVLEGLGALD DVLQGSHTPP TYETWMHNKS VSKETFNGLP
110 120 130 140 150
WRIMTRSHLH DALVNRARAL GVDISVNSEA VAADPVGRLT LQTGEVLEAD
160 170 180 190 200
LIVGADGVGS KVRDSIGFKQ DRWVSKDGLI RLIVPRMKKE LGHGEWDNTI
210 220 230 240 250
DMWNFWPRVQ RILYSPCNEN ELYLGLMAPA ADPRGSSVPI DLEVWVEMFP
260 270 280 290 300
FLEPCLIEAA KLKTARYDKY ETTKLDSWTR GKVALVGDAA HAMCPALAQG
310 320 330 340 350
AGCAMVNAFS LSQDLEEGSS VEDALVAWET RIRPITDRCQ ALSGDYAANR
360 370
SLSKGNMFTP AALEAARYDP LRRVYSWPQ
Length:379
Mass (Da):41,748
Last modified:October 1, 2001 - v1
Checksum:i297E85523850E499
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB53017.1.
RefSeqiWP_010914327.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB53017; BAB53017; BAB53017.
GeneIDi1229886.
KEGGimlo:mlr6788.
PATRICi22485043. VBIMesLot2464_5401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB53017.1.
RefSeqiWP_010914327.1. NC_002678.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ALJX-ray1.48A1-379[»]
3ALLX-ray1.78A/B1-379[»]
3ALMX-ray1.77A/B1-379[»]
3GMBX-ray2.10A/B1-379[»]
3GMCX-ray2.10A/B1-379[»]
4GF7X-ray1.58A1-379[»]
4H2NX-ray2.30A1-379[»]
4H2PX-ray1.98A/B/C/D1-379[»]
4H2QX-ray1.50A1-379[»]
4H2RX-ray2.47A/B1-379[»]
4JY2X-ray1.94A/B1-379[»]
4JY3X-ray1.77A/B1-379[»]
ProteinModelPortaliQ988D3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266835.mlr6788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB53017; BAB53017; BAB53017.
GeneIDi1229886.
KEGGimlo:mlr6788.
PATRICi22485043. VBIMesLot2464_5401.

Phylogenomic databases

HOGENOMiHOG000000640.
KOiK18071.
OMAiCNENELY.
OrthoDBiEOG6J48MG.

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-5382-MONOMER.
BRENDAi1.14.12.4. 3243.

Miscellaneous databases

EvolutionaryTraceiQ988D3.

Family and domain databases

InterProiIPR002938. mOase_FAD-bd.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MAFF303099Imported.
  2. "Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications."
    McCulloch K.M., Mukherjee T., Begley T.P., Ealick S.E.
    Biochemistry 48:4139-4149(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  3. "Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Yoshikane Y., Kamitori S., Yagi T.
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH FAD.
  4. "Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Mikami B., Hayashi H., Kamitori S., Sawa Y., Yagi T.
    Submitted (AUG-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEX WITH FAD.
  5. "Crystal structure of 2-Methyl-3-hydroxypyridiine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Mikami B., Hayashi H., Kamitori S., Yagi T.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FAD.
  6. "Crystal structure of 2-Methyl-3-hydroxypyridine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Mikami B., Hayashi H., Kamitori S., Yagi T.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) IN COMPLEX WITH FAD.
  7. "Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Mikami B., Hayashi H., Kamitori S., Yagi T.
    Submitted (SEP-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FAD.
  8. "Crystal structure of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase."
    Kobayashi J., Yoshida H., Kamitori S., Hayashi H., Mizutani K., Takahashi N., Mikami B., Yagi T.
    Submitted (MAR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).

Entry informationi

Entry nameiQ988D3_RHILO
AccessioniPrimary (citable) accession number: Q988D3
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2001
Last sequence update: October 1, 2001
Last modified: July 22, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, 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.