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Q59327 (OASD_COMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
3-oxo-5-alpha-steroid 4-dehydrogenase

EC=1.3.99.5
Alternative name(s):
Delta 4, 5-alpha steroid dehydrogenase
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A. Ref.1

Catalytic activity

A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor. Ref.1

5-alpha-androstane-3,17-dione + acceptor = 5-alpha-4-androstene-3,17-dione + reduced acceptor. Ref.1

5-alpha-1-androstene-3,17-dione + acceptor = 1,4-androstadiene-3,17-dione + reduced acceptor. Ref.1

Cofactor

FAD Probable. Ref.1

Enzyme regulation

Inhibition occurrs with substrate concentrations above 25 µM. Ref.1

Subcellular location

Membrane; Single-pass membrane protein Potential Ref.1 Ref.2.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=6.6 µM for 5-alpha-1-androstene-3,17-dione (at 30 degrees Celsius and at pH 8.2) Ref.1

KM=16.1 µM for 5-alpha-androstane-3,17-dione (at 30 degrees Celsius and at pH 8.2)

Vmax=456 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as substrate (at 30 degrees Celsius and at pH 8.2)

Vmax=700 nmol/min/mg enzyme with 5-alpha-1-androstene-3,17-dione as substrate (at 30 degrees Celsius and at pH 8.2)

pH dependence:

Optimum pH is 8.

Temperature dependence:

Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
   Biological processLipid metabolism
Steroid metabolism
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processsteroid catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3-oxo-5-alpha-steroid 4-dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-oxosteroid 1-dehydrogenase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5305303-oxo-5-alpha-steroid 4-dehydrogenase
PRO_0000418533

Regions

Transmembrane395 – 41521Helical; Potential
Nucleotide binding33 – 6230FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59327 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5E5D6CEAC0BF2EC1

FASTA53057,289
        10         20         30         40         50         60 
MSNVKKHVST INPVGEVLDV GSADEVQWSD ASDVVVVGWG GAGASAAIEA REQGAEVLVI 

        70         80         90        100        110        120 
ERFSGGGASV LSGGVVYAGA VPATRRKPAS RFTEAMTAYL KHEVNGVVSD ETLARFSRDS 

       130        140        150        160        170        180 
VTNLNWLEKQ GATFASTMPG YKTSYPADGM YLYYSGNEVV PAYGNPQLLK KPPPRGHRVV 

       190        200        210        220        230        240 
AKGQSGAMFF AALQKSTLAH GARTLTQARV QRLVREKDSG RVLGVEVMVL PEGDPRTERH 

       250        260        270        280        290        300 
KKLDELVAKS ACIRRRVPRR VAVNVRRSRA RSARSATSVP AKVWCCPLAA ISSIRNCWSM 

       310        320        330        340        350        360 
RRYKPGWLTG AAGCDGSGLR LGQSVGGIAQ DLNNISAWRF ITPPSVWPKG LVVNIQGERF 

       370        380        390        400        410        420 
CNEQVYGAKL GYEMMEKQGG QAWLIIDSNV RRQAAWQCLF GGLWAFQSMP ALALMYKVAI 

       430        440        450        460        470        480 
KGKSVDDLAK KLRMDAAVLQ LQFDRANAPA RGEIEDPLGK SQDMRHEFKG GSLFAIDISI 

       490        500        510        520        530 
SQKMFPLAVL SLGGLKVNED NGAVIDGAGY DIPGLYAAGV PPLVWLPRVT 

« Hide

References

[1]"Comamonas testosteroni 3-ketosteroid-delta 4(5 alpha)-dehydrogenase: gene and protein characterization."
Florin C., Kohler T., Grandguillot M., Plesiat P.
J. Bacteriol. 178:3322-3330(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, COFACTOR, SUBSTRATE SPECIFICITY.
[2]"Bacterial oxidation of steroids. II. Studies on the enzymatic mechanism of ring A dehydrogenation."
Levy H.R., Talalay P.
J. Biol. Chem. 234:2014-2021(1959) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23428 Genomic DNA. Translation: AAB08517.1.
PIRJC6030.

3D structure databases

ProteinModelPortalQ59327.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16925.

Family and domain databases

Gene3D3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
SUPFAMSSF56425. SSF56425. 1 hit.
ProtoNetSearch...

Entry information

Entry nameOASD_COMTE
AccessionPrimary (citable) accession number: Q59327
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 66 of the entry and version 1 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