Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q988D3

- Q988D3_RHILO

UniProt

Q988D3 - Q988D3_RHILO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Submitted name:

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

Gene

mlr6788

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Unreviewed - 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 oxygenImported
Binding sitei106 – 1061FADImported
Binding sitei130 – 1301FAD; via amide nitrogen and carbonyl oxygenImported
Binding sitei156 – 1561FAD; via carbonyl oxygenImported
Binding sitei181 – 1811FADImported
Binding sitei288 – 2881FADImported

Regions

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

GO - Molecular functioni

  1. nucleotide binding Source: UniProtKB-KW
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

FADImported, Flavoprotein, Nucleotide-bindingImported

Enzyme and pathway databases

BioCyciMLOT266835:GJ9L-5382-MONOMER.

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: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi266835.mlr6788.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSiPR00420. RNGMNOXGNASE.

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:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB53017.1.
RefSeqiNP_107231.1. NC_002678.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB53017.1 .
RefSeqi NP_107231.1. NC_002678.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ALJ X-ray 1.48 A 1-379 [» ]
3ALL X-ray 1.78 A/B 1-379 [» ]
3ALM X-ray 1.77 A/B 1-379 [» ]
3GMB X-ray 2.10 A/B 1-379 [» ]
3GMC X-ray 2.10 A/B 1-379 [» ]
4GF7 X-ray 1.58 A 1-379 [» ]
4H2N X-ray 2.30 A 1-379 [» ]
4H2P X-ray 1.98 A/B/C/D 1-379 [» ]
4H2Q X-ray 1.50 A 1-379 [» ]
4H2R X-ray 2.47 A/B 1-379 [» ]
4JY2 X-ray 1.94 A/B 1-379 [» ]
4JY3 X-ray 1.77 A/B 1-379 [» ]
ProteinModelPortali Q988D3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266835.mlr6788.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB53017 ; BAB53017 ; BAB53017 .
GeneIDi 1229886.
KEGGi mlo:mlr6788.
PATRICi 22485043. VBIMesLot2464_5401.

Phylogenomic databases

HOGENOMi HOG000000640.
KOi K18071.
OMAi CNENELY.
OrthoDBi EOG6J48MG.

Enzyme and pathway databases

BioCyci MLOT266835:GJ9L-5382-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q988D3.

Family and domain databases

InterProi IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view ]
Pfami PF01494. FAD_binding_3. 1 hit.
[Graphical view ]
PRINTSi PR00420. RNGMNOXGNASE.
ProtoNeti Search...

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 (1.78 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: October 29, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3