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Q59327

- OASD_COMTE

UniProt

Q59327 - OASD_COMTE

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Protein
3-oxo-5-alpha-steroid 4-dehydrogenase
Gene
N/A
Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor.1 Publication
5-alpha-androstane-3,17-dione + acceptor = 5-alpha-4-androstene-3,17-dione + reduced acceptor.1 Publication
5-alpha-1-androstene-3,17-dione + acceptor = 1,4-androstadiene-3,17-dione + reduced acceptor.1 Publication

Cofactori

FAD Inferred.1 Publication

Enzyme regulationi

Inhibition occurrs with substrate concentrations above 25 µM.1 Publication

Kineticsi

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

Optimum pH is 8.

Temperature dependencei

Optimum temperature is 40 degrees Celsius.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 6230FAD By similarity
Add
BLAST

GO - Molecular functioni

  1. 3-oxo-5-alpha-steroid 4-dehydrogenase activity Source: UniProtKB-EC
  2. 3-oxosteroid 1-dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. steroid catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16925.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxo-5-alpha-steroid 4-dehydrogenase (EC:1.3.99.5)
Alternative name(s):
Delta 4, 5-alpha steroid dehydrogenase
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Subcellular locationi

Membrane; Single-pass membrane protein Reviewed prediction 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei395 – 41521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5305303-oxo-5-alpha-steroid 4-dehydrogenase
PRO_0000418533Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ59327.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.700.10. 1 hit.
InterProiIPR003953. FAD_bind_dom.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF56425. SSF56425. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59327-1 [UniParc]FASTAAdd to Basket

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MSNVKKHVST INPVGEVLDV GSADEVQWSD ASDVVVVGWG GAGASAAIEA    50
REQGAEVLVI ERFSGGGASV LSGGVVYAGA VPATRRKPAS RFTEAMTAYL 100
KHEVNGVVSD ETLARFSRDS VTNLNWLEKQ GATFASTMPG YKTSYPADGM 150
YLYYSGNEVV PAYGNPQLLK KPPPRGHRVV AKGQSGAMFF AALQKSTLAH 200
GARTLTQARV QRLVREKDSG RVLGVEVMVL PEGDPRTERH KKLDELVAKS 250
ACIRRRVPRR VAVNVRRSRA RSARSATSVP AKVWCCPLAA ISSIRNCWSM 300
RRYKPGWLTG AAGCDGSGLR LGQSVGGIAQ DLNNISAWRF ITPPSVWPKG 350
LVVNIQGERF CNEQVYGAKL GYEMMEKQGG QAWLIIDSNV RRQAAWQCLF 400
GGLWAFQSMP ALALMYKVAI KGKSVDDLAK KLRMDAAVLQ LQFDRANAPA 450
RGEIEDPLGK SQDMRHEFKG GSLFAIDISI SQKMFPLAVL SLGGLKVNED 500
NGAVIDGAGY DIPGLYAAGV PPLVWLPRVT 530
Length:530
Mass (Da):57,289
Last modified:November 1, 1996 - v1
Checksum:i5E5D6CEAC0BF2EC1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23428 Genomic DNA. Translation: AAB08517.1.
PIRiJC6030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23428 Genomic DNA. Translation: AAB08517.1 .
PIRi JC6030.

3D structure databases

ProteinModelPortali Q59327.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16925.

Family and domain databases

Gene3Di 3.90.700.10. 1 hit.
InterProi IPR003953. FAD_bind_dom.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
[Graphical view ]
Pfami PF00890. FAD_binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56425. SSF56425. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiOASD_COMTE
AccessioniPrimary (citable) accession number: Q59327
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3