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Q59327

- OASD_COMTE

UniProt

Q59327 - OASD_COMTE

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
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.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)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

    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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    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...

    Transmembrane

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

    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

    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: October 1, 2014
    This is version 67 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