Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q59472 (Q59472_KLEOX) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
EC=4.2.1.28 EMBL BAA08101.1
Gene names
Name:pddC EMBL BAA08101.1
OrganismKlebsiella oxytoca EMBL BAA08101.1
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region75 – 773Phosphate 1 binding PDB 3AUJ
Region75 – 773Phosphate 2 binding PDB 3AUJ

Sequences

Sequence LengthMass (Da)Tools
Q59472 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0B8602E39B38ECD0

FASTA17319,173
        10         20         30         40         50         60 
MNTDAIESMV RDVLSRMNSL QGEAPAAAPA AGGASRSARV SDYPLANKHP EWVKTATNKT 

        70         80         90        100        110        120 
LDDFTLENVL SNKVTAQDMR ITPETLRLQA SIAKDAGRDR LAMNFERAAE LTAVPDDRIL 

       130        140        150        160        170 
EIYNALRPYR STKEELLAIA DDLESRYQAK ICAAFVREAA TLYVERKKLK GDD 

« Hide

References

[1]"Molecular cloning, sequencing, and expression of the genes encoding adenosylcobalamin-dependent diol dehydrase of Klebsiella oxytoca."
Tobimatsu T., Hara T., Sakaguchi M., Kishimoto Y., Wada Y., Isoda M., Sakai T., Toraya T.
J. Biol. Chem. 270:7142-7148(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 8724 EMBL BAA08101.1.
[2]"A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase."
Shibata N., Masuda J., Tobimatsu T., Toraya T., Suto K., Morimoto Y., Yasuoka N.
Structure 7:997-1008(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
[3]"How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex."
Masuda J., Shibata N., Morimoto Y., Toraya T., Yasuoka N.
Structure 8:775-788(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
[4]"Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase."
Shibata N., Masuda J., Morimoto Y., Yasuoka N., Toraya T.
Biochemistry 41:12607-12617(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[5]"Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase."
Shibata N., Nakanishi Y., Fukuoka M., Yamanishi M., Yasuoka N., Toraya T.
J. Biol. Chem. 278:22717-22725(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
[6]"Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols."
Yamanishi M., Kinoshita K., Fukuoka M., Saito T., Tanokuchi A., Ikeda Y., Obayashi H., Mori K., Shibata N., Tobimatsu T., Toraya T.
FEBS J. 279:793-804(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45071 Genomic DNA. Translation: BAA08101.1.
PIRC56111.
RefSeqYP_005016277.1. NC_016612.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DIOX-ray2.20G/M1-173[»]
1EEXX-ray1.70G/M1-173[»]
1EGMX-ray1.85G/M1-173[»]
1EGVX-ray1.75G/M1-173[»]
1IWBX-ray1.85G/M1-173[»]
1UC4X-ray1.80G/M1-173[»]
1UC5X-ray2.30G/M1-173[»]
3AUJX-ray2.10G/M1-173[»]
ProteinModelPortalQ59472.
SMRQ59472. Positions 37-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ59472. 2 interactions.
MINTMINT-7997129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11660427.
KEGGkox:KOX_01465.

Phylogenomic databases

KOK13920.

Family and domain databases

InterProIPR003207. Ppandiol/glycerol_DeHydtase_su.
[Graphical view]
PfamPF02287. Dehydratase_SU. 1 hit.
[Graphical view]
PIRSFPIRSF018505. Prpndl_dhdrts_sm. 1 hit.
SUPFAMSSF47148. SSF47148. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ59472.

Entry information

Entry nameQ59472_KLEOX
AccessionPrimary (citable) accession number: Q59472
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)