3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase

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P80702 (DIDH_COMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase
Short name=3-alpha-HSD
EC=1.1.1.50

Alternative name(s):
3-alpha-hydroxysteroid dehydrogenase/3-oxosteroid reductase
HSD28
Hydroxyprostaglandin dehydrogenase

Gene names

Name:

hsdA

Organism

Comamonas testosteroni (Pseudomonas testosteroni)

Taxonomic identifier

285 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible interconversion of hydroxy and oxo groups at position 3 of the steroid nucleus. Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. No detectable activity on testosterone, progesterone or 3-oxo-desogestrel.
Catalytic activity	Androsterone + NAD(P)⁺ = 5-alpha-androstane-3,17-dione + NAD(P)H.
Subunit structure	Homodimer. Ref.3 Ref.5
Subcellular location	Cytoplasm Ref.2.
Induction	By steroids. Derepression of gene transcription occurs by binding of the steroid inducer molecule to a repressor protein. Ref.2 Ref.4
Miscellaneous	This protein is thought to initiate prokaryotic steroid catabolism.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Biophysicochemical properties	Kinetic parameters: K_M=35.7 µM for androstandione Ref.2 Ref.3 K_M=24.4 µM for androsterone K_M=3.0 µM for fusidic acid K_M=610 µM for metyrapone V_max=52.3 µmol/min/mg enzyme for androstandione V_max=10.3 µmol/min/mg enzyme for androsterone V_max=18.1 µmol/min/mg enzyme fusidic acid V_max=0.63 µmol/min/mg enzyme metyrapone

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	androsterone dehydrogenase (B-specific) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 257

256

3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase

PRO_0000054656

Regions

Nucleotide binding

8 – 13

NAD

Nucleotide binding

41 – 42

NAD

Sites

Active site

155

Proton acceptor By similarity

Binding site

NAD

Binding site

NAD; via amide nitrogen

Binding site

114

Substrate By similarity

Binding site

155

NAD

Binding site

159

NAD

Experimental info

Sequence conflict

S → D AA sequence Ref.2

Sequence conflict

C → A AA sequence Ref.2

Sequence conflict

R → C AA sequence Ref.2

Sequence conflict

H → S AA sequence Ref.2

Sequence conflict

G → S AA sequence Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P80702 [UniParc].

Last modified December 14, 2011. Version 2.
Checksum: 65B6F19444F20EFE
Show »

FASTA

257

26,392

        10         20         30         40         50         60 
MSIIVISGCA TGIGAATRKV LEAAGHQIVG IDIRDAEVIA DLSTAEGRKQ AIADVLAKCS 

        70         80         90        100        110        120 
KGMDGLVLCA GLGPQTKVLG NVVSVNYFGA TELMDAFLPA LKKGHQPAAV VISSVASAHL 

       130        140        150        160        170        180 
AFDKNPLALA LEAGEEAKAR AIVEHAGEQG GNLAYAGSKN ALTVAVRKRA AAWGEAGVRL 

       190        200        210        220        230        240 
NTIAPGATET PLLQAGLQDP RYGESIAKFV PPMGRRAEPS EMASVIAFLM SPAASYVHGA 

       250 
QIVIDGGIDA VMRPTQF

« Hide

References

[1]	"Molecular cloning, overexpression, and characterization of steroid-inducible 3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily." Mobus E., Maser E. J. Biol. Chem. 273:30888-30896(1998) [PubMed: 9812981] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698.
[2]	"Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase from the Gram-negative bacterium Comamonas testosteroni." Oppermann U.C.T., Maser E. Eur. J. Biochem. 241:744-749(1996) [PubMed: 8944761] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION. Strain: ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698.
[3]	"Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni." Maser E., Mobus E., Xiong G. Biochem. Biophys. Res. Commun. 272:622-628(2000) [PubMed: 10833462] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[4]	"Regulation of the steroid-inducible 3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni." Xiong G., Maser E. J. Biol. Chem. 276:9961-9970(2001) [PubMed: 11139589] [Abstract] Cited for: INDUCTION. Strain: ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698.
[5]	"The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family." Grimm C., Maser E., Mobus E., Klebe G., Reuter K., Ficner R. J. Biol. Chem. 275:41333-41339(2000) [PubMed: 11007791] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) ALONE AND IN COMPLEX WITH NAD, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF092031 Genomic DNA. Translation: AAC79849.1.

PIR

JC7291.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJH	X-ray	1.68	A/B	1-257	[»]
1FK8	X-ray	1.95	A/B	1-257	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PRINTS

PR00081. GDHRDH.

PROSITE

PS00061. ADH_SHORT. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DIDH_COMTE

Accession

Primary (citable) accession number: P80702
Secondary accession number(s): Q9ZFY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 14, 2011
Last modified:	January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents