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P20906 (MDLC_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Benzoylformate decarboxylase

Short name=BFD
Short name=BFDC
EC=4.1.1.7
Gene names
Name:mdlC
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Benzoylformate = benzaldehyde + CO2.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 thiamine pyrophosphate per subunit.

Binds 1 magnesium ion per dimer.

Pathway

Aromatic compound metabolism; (R)-mandelate degradation; benzoate from (R)-mandelate: step 3/4.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Benzoylformate decarboxylase
PRO_0000090820

Regions

Region377 – 46084Thiamine pyrophosphate binding

Sites

Metal binding1171Magnesium; via carbonyl oxygen
Metal binding1181Magnesium; via carbonyl oxygen
Metal binding1201Magnesium
Metal binding4281Calcium
Metal binding4551Calcium
Metal binding4571Calcium

Secondary structure

............................................................................................... 528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20906 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: DDB7BC03AD866CC1

FASTA52856,355
        10         20         30         40         50         60 
MASVHGTTYE LLRRQGIDTV FGNPGSNELP FLKDFPEDFR YILALQEACV VGIADGYAQA 

        70         80         90        100        110        120 
SRKPAFINLH SAAGTGNAMG ALSNAWNSHS PLIVTAGQQT RAMIGVEALL TNVDAANLPR 

       130        140        150        160        170        180 
PLVKWSYEPA SAAEVPHAMS RAIHMASMAP QGPVYLSVPY DDWDKDADPQ SHHLFDRHVS 

       190        200        210        220        230        240 
SSVRLNDQDL DILVKALNSA SNPAIVLGPD VDAANANADC VMLAERLKAP VWVAPSAPRC 

       250        260        270        280        290        300 
PFPTRHPCFR GLMPAGIAAI SQLLEGHDVV LVIGAPVFRY HQYDPGQYLK PGTRLISVTC 

       310        320        330        340        350        360 
DPLEAARAPM GDAIVADIGA MASALANLVE ESSRQLPTAA PEPAKVDQDA GRLHPETVFD 

       370        380        390        400        410        420 
TLNDMAPENA IYLNESTSTT AQMWQRLNMR NPGSYYFCAA GGLGFALPAA IGVQLAEPER 

       430        440        450        460        470        480 
QVIAVIGDGS ANYSISALWT AAQYNIPTIF VIMNNGTYGA LRWFAGVLEA ENVPGLDVPG 

       490        500        510        520 
IDFRALAKGY GVQALKADNL EQLKGSLQEA LSAKGPVLIE VSTVSPVK 

« Hide

References

[1]"Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli."
Tsou A.Y., Ransom S.C., Gerlt J.A., Buechter D.D., Babbitt P.C., Kenyon G.L.
Biochemistry 29:9856-9862(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19.
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
[2]"Purification and crystallization of benzoylformate decarboxylase."
Hasson M.S., Muscate A., Henehan G.T.M., Guidinger P.F., Petsko G.A., Ringe D., Kenyon G.L.
Protein Sci. 4:955-959(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
[3]"The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes."
Hasson M.S., Muscate A., McLeish M.J., Polovnikova L.S., Gerlt J.A., Kenyon G.L., Petsko G.A., Ringe D.
Biochemistry 37:9918-9930(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SEQUENCE REVISION TO C-TERMINUS.
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY143338 Genomic DNA. Translation: AAC15502.1.
PIRC44767.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BFDX-ray1.60A1-528[»]
1MCZX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-528[»]
1PI3X-ray1.20A1-528[»]
1PO7X-ray1.20A1-528[»]
1Q6ZX-ray1.00A1-528[»]
1YNOX-ray1.22A2-528[»]
2FN3X-ray1.00A1-528[»]
2FWNX-ray1.40A1-528[»]
2V3WX-ray2.20A/B/C/D1-528[»]
3F6BX-ray1.34X2-526[»]
3F6EX-ray1.34X2-526[»]
3FSJX-ray1.37X1-528[»]
3FZNX-ray1.62A/B/C/D1-528[»]
4GG1X-ray1.07A1-528[»]
4GM0X-ray1.07A1-528[»]
4GM1X-ray1.26A1-528[»]
4GM4X-ray1.28A1-528[»]
4GP9X-ray1.07A1-528[»]
4GPEX-ray1.39A1-528[»]
4JD5X-ray1.33A1-528[»]
4JU8X-ray1.25A1-528[»]
4JU9X-ray1.12A1-528[»]
4JUAX-ray1.15A1-528[»]
4JUBX-ray1.90A/B/C/D1-528[»]
4JUCX-ray2.30A/B/C/D1-528[»]
4JUDX-ray1.65X1-528[»]
4JUFX-ray2.15A/B/C/D2-528[»]
4K9KX-ray1.30A2-525[»]
4K9LX-ray1.65A2-526[»]
4K9MX-ray1.15A2-525[»]
4K9NX-ray1.70A/B/C/D2-525[»]
4K9OX-ray1.89A/B/C/D2-528[»]
4K9PX-ray2.24A/B/C/D2-528[»]
ProteinModelPortalP20906.
SMRP20906. Positions 2-525.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2461.
SABIO-RKP20906.
UniPathwayUPA00873; UER00854.

Family and domain databases

Gene3D3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20906.

Entry information

Entry nameMDLC_PSEPU
AccessionPrimary (citable) accession number: P20906
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways