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Protein

3-beta-hydroxysteroid dehydrogenase

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

Functioni

Catalytic activityi

Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei61NADBy similarity1
Binding sitei139SubstrateBy similarity1
Active sitei152Proton acceptorPROSITE-ProRule annotation1
Binding sitei156NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 40NADBy similarityAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16923.
BRENDAi1.1.1.51. 1590.

Names & Taxonomyi

Protein namesi
Recommended name:
3-beta-hydroxysteroid dehydrogenase (EC:1.1.1.51)
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000544462 – 2543-beta-hydroxysteroid dehydrogenaseAdd BLAST253

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi688245.CtCNB1_1764.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Beta strandi9 – 12Combined sources4
Turni13 – 16Combined sources4
Helixi18 – 29Combined sources12
Beta strandi33 – 37Combined sources5
Helixi41 – 51Combined sources11
Beta strandi55 – 58Combined sources4
Helixi65 – 79Combined sources15
Beta strandi84 – 87Combined sources4
Turni97 – 99Combined sources3
Helixi102 – 112Combined sources11
Helixi114 – 127Combined sources14
Turni128 – 130Combined sources3
Beta strandi132 – 137Combined sources6
Helixi140 – 142Combined sources3
Helixi150 – 173Combined sources24
Beta strandi177 – 187Combined sources11
Helixi190 – 195Combined sources6
Helixi202 – 205Combined sources4
Turni209 – 211Combined sources3
Helixi220 – 231Combined sources12
Helixi233 – 235Combined sources3
Beta strandi242 – 248Combined sources7
Turni250 – 253Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HXHX-ray1.22A/B/C/D2-254[»]
ProteinModelPortaliP19871.
SMRiP19871.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19871.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105V9V. Bacteria.
COG1028. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNRLQGKVA LVTGGASGVG LEVVKLLLGE GAKVAFSDIN EAAGQQLAAE
60 70 80 90 100
LGERSMFVRH DVSSEADWTL VMAAVQRRLG TLNVLVNNAG ILLPGDMETG
110 120 130 140 150
RLEDFSRLLK INTESVFIGC QQGIAAMKET GGSIINMASV SSWLPIEQYA
160 170 180 190 200
GYSASKAAVS ALTRAAALSC RKQGYAIRVN SIHPDGIYTP MMQASLPKGV
210 220 230 240 250
SKEMVLHDPK LNRAGRAYMP ERIAQLVLFL ASDESSVMSG SELHADNSIL

GMGL
Length:254
Mass (Da):26,952
Last modified:January 23, 2007 - v5
Checksum:iFB6EC90B151975DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15GG → VV in CAA44977 (PubMed:8382516).Curated2
Sequence conflicti41Missing in CAA44977 (PubMed:8382516).Curated1
Sequence conflicti178R → RR in CAA44977 (PubMed:8382516).Curated1
Sequence conflicti241S → G AA sequence (PubMed:2026158).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63379 Genomic DNA. Translation: CAA44977.1.
U41265 Genomic DNA. Translation: AAA25742.1.
PIRiS48129.
RefSeqiWP_003080542.1. NZ_BBJZ01000009.1.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63379 Genomic DNA. Translation: CAA44977.1.
U41265 Genomic DNA. Translation: AAA25742.1.
PIRiS48129.
RefSeqiWP_003080542.1. NZ_BBJZ01000009.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HXHX-ray1.22A/B/C/D2-254[»]
ProteinModelPortaliP19871.
SMRiP19871.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi688245.CtCNB1_1764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105V9V. Bacteria.
COG1028. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16923.
BRENDAi1.1.1.51. 1590.

Miscellaneous databases

EvolutionaryTraceiP19871.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei3BHD_COMTE
AccessioniPrimary (citable) accession number: P19871
Secondary accession number(s): Q52587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.