[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; DOI=10.1016/0960-0760(93)90020-W; PubMed=8382516 [NCBI, ExPASy, EBI, Israel, Japan] Abalain J.H., di Stefano S., Amet Y., Quemener E., Abalain-Colloc M.L., Floch H.H.; "Cloning, DNA sequencing and expression of (3-17)beta hydroxysteroid dehydrogenase from Pseudomonas testosteroni."; J. Steroid Biochem. Mol. Biol. 44:133-139(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; DOI=10.1016/j.jsbmb.2003.10.010; PubMed=15026087 [NCBI, ExPASy, EBI, Israel, Japan] Pruneda-Paz J.L., Linares M., Cabrera J.E., Genti-Raimondi S.; "Identification of a novel steroid inducible gene associated with the beta hsd locus of Comamonas testosteroni."; J. Steroid Biochem. Mol. Biol. 88:91-100(2004).
[3]	PROTEIN SEQUENCE OF 2-254. DOI=10.1111/j.1432-1033.1991.tb15919.x; PubMed=2026158 [NCBI, ExPASy, EBI, Israel, Japan] Yin S.-J., Vagelopoulos N., Lundquist G., Joernvall H.; "Pseudomonas 3 beta-hydroxysteroid dehydrogenase. Primary structure and relationships to other steroid dehydrogenases."; Eur. J. Biochem. 197:359-365(1991).
[4]	CRYSTALLIZATION, AND SUBUNIT. STRAIN=ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698; DOI=10.1111/j.1432-1033.1996.t01-1-00144.x; PubMed=8617258 [NCBI, ExPASy, EBI, Israel, Japan] Benach J., Knapp S., Oppermann U.C.T., Haegllund O., Joernvall H., Ladenstein R.; "Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996."; Eur. J. Biochem. 236:144-148(1996).
[5]	X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS). DOI=10.1021/bi0203684; PubMed=12475215 [NCBI, ExPASy, EBI, Israel, Japan] Benach J., Filling C., Oppermann U.C.T., Roversi P., Bricogne G., Berndt K.D., Joernvall H., Ladenstein R.; "Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition."; Biochemistry 41:14659-14668(2002).

Comments

CATALYTIC ACTIVITY: Testosterone + NAD(P)⁺ = androst-4-ene-3,17-dione + NAD(P)H.
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/STDH/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X63379; CAA44977.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41265; AAA25742.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48129; S48129.

3D structure databases

PDB

1HXH; X-ray; 1.22 A; A/B/C/D=1-254.

[ExPASy / RCSB / EBI]

PDBsum

1HXH; -.

ModBase

P19871.

Ontologies

GO:0030283;	Molecular function: 3(or 17)beta-hydroxysteroid dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008202;	Biological process: steroid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Other

ProtoNet

P19871.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Lipid metabolism; NAD; Oxidoreductase; Steroid metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 254`	`253`	`3-beta-hydroxysteroid dehydrogenase.`	`PRO_0000054446`
`NP_BIND`	`12 40`	`29`	`NAD (By similarity).`
`ACT_SITE`	`152 152`		`Proton acceptor (By similarity).`
`BINDING`	`61 61`		`NAD (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`BINDING`	`156 156`		`NAD (By similarity).`
`CONFLICT`	`14 15`		`GG -> VV (in Ref. 1; CAA44977).`
`CONFLICT`	`41 41`		`Missing (in Ref. 1; CAA44977).`
`CONFLICT`	`178 178`		`R -> RR (in Ref. 1; CAA44977).`
`CONFLICT`	`241 241`		`S -> G (in Ref. 3; AA sequence).`
`TURN`	`4 7`	`4`
`STRAND`	`9 12`	`4`
`TURN`	`13 16`	`4`
`HELIX`	`18 29`	`12`
`STRAND`	`33 37`	`5`
`HELIX`	`41 51`	`11`
`STRAND`	`55 58`	`4`
`HELIX`	`65 79`	`15`
`STRAND`	`84 87`	`4`
`TURN`	`97 99`	`3`
`HELIX`	`102 112`	`11`
`HELIX`	`114 127`	`14`
`TURN`	`128 130`	`3`
`STRAND`	`132 137`	`6`
`HELIX`	`140 142`	`3`
`HELIX`	`150 173`	`24`
`STRAND`	`177 187`	`11`
`HELIX`	`190 195`	`6`
`HELIX`	`202 205`	`4`
`TURN`	`209 211`	`3`
`HELIX`	`220 231`	`12`
`HELIX`	`233 235`	`3`
`STRAND`	`242 248`	`7`
`TURN`	`250 253`	`4`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 26952 Da [This is the MW of the unprocessed precursor]

CRC64: FB6EC90B151975DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNRLQGKVA LVTGGASGVG LEVVKLLLGE GAKVAFSDIN EAAGQQLAAE LGERSMFVRH 

        70         80         90        100        110        120 
DVSSEADWTL VMAAVQRRLG TLNVLVNNAG ILLPGDMETG RLEDFSRLLK INTESVFIGC 

       130        140        150        160        170        180 
QQGIAAMKET GGSIINMASV SSWLPIEQYA GYSASKAAVS ALTRAAALSC RKQGYAIRVN 

       190        200        210        220        230        240 
SIHPDGIYTP MMQASLPKGV SKEMVLHDPK LNRAGRAYMP ERIAQLVLFL ASDESSVMSG 

       250 
SELHADNSIL GMGL

P19871 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools