Skip Header

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

Q59327

- OASD_COMTE

UniProt

Q59327 - OASD_COMTE

(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

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

FAD1 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)1 Publication

Vmax=456 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as substrate (at 30 degrees Celsius and at pH 8.2)1 Publication

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)1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 6230FADBy similarityAdd
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei395 – 41521HelicalSequence AnalysisAdd
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-dehydrogenasePRO_0000418533Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ59327.
ModBaseiSearch...
MobiDBiSearch...

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

« Hide

        10         20         30         40         50
MSNVKKHVST INPVGEVLDV GSADEVQWSD ASDVVVVGWG GAGASAAIEA
60 70 80 90 100
REQGAEVLVI ERFSGGGASV LSGGVVYAGA VPATRRKPAS RFTEAMTAYL
110 120 130 140 150
KHEVNGVVSD ETLARFSRDS VTNLNWLEKQ GATFASTMPG YKTSYPADGM
160 170 180 190 200
YLYYSGNEVV PAYGNPQLLK KPPPRGHRVV AKGQSGAMFF AALQKSTLAH
210 220 230 240 250
GARTLTQARV QRLVREKDSG RVLGVEVMVL PEGDPRTERH KKLDELVAKS
260 270 280 290 300
ACIRRRVPRR VAVNVRRSRA RSARSATSVP AKVWCCPLAA ISSIRNCWSM
310 320 330 340 350
RRYKPGWLTG AAGCDGSGLR LGQSVGGIAQ DLNNISAWRF ITPPSVWPKG
360 370 380 390 400
LVVNIQGERF CNEQVYGAKL GYEMMEKQGG QAWLIIDSNV RRQAAWQCLF
410 420 430 440 450
GGLWAFQSMP ALALMYKVAI KGKSVDDLAK KLRMDAAVLQ LQFDRANAPA
460 470 480 490 500
RGEIEDPLGK SQDMRHEFKG GSLFAIDISI SQKMFPLAVL SLGGLKVNED
510 520 530
NGAVIDGAGY DIPGLYAAGV PPLVWLPRVT
Length:530
Mass (Da):57,289
Last modified:November 1, 1996 - v1
Checksum:i5E5D6CEAC0BF2EC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23428 Genomic DNA. Translation: AAB08517.1.
PIRiJC6030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 68 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