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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611NADBy similarity
Binding sitei139 – 1391SubstrateBy similarity
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation
Binding sitei156 – 1561NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 4029NADBy similarityAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 2542533-beta-hydroxysteroid dehydrogenasePRO_0000054446Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi688245.CtCNB1_1764.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi9 – 124Combined sources
Turni13 – 164Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 375Combined sources
Helixi41 – 5111Combined sources
Beta strandi55 – 584Combined sources
Helixi65 – 7915Combined sources
Beta strandi84 – 874Combined sources
Turni97 – 993Combined sources
Helixi102 – 11211Combined sources
Helixi114 – 12714Combined sources
Turni128 – 1303Combined sources
Beta strandi132 – 1376Combined sources
Helixi140 – 1423Combined sources
Helixi150 – 17324Combined sources
Beta strandi177 – 18711Combined sources
Helixi190 – 1956Combined sources
Helixi202 – 2054Combined sources
Turni209 – 2113Combined sources
Helixi220 – 23112Combined sources
Helixi233 – 2353Combined sources
Beta strandi242 – 2487Combined sources
Turni250 – 2534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXHX-ray1.22A/B/C/D2-254[»]
ProteinModelPortaliP19871.
SMRiP19871. Positions 2-254.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152GG → VV in CAA44977 (PubMed:8382516).Curated
Sequence conflicti41 – 411Missing in CAA44977 (PubMed:8382516).Curated
Sequence conflicti178 – 1781R → RR in CAA44977 (PubMed:8382516).Curated
Sequence conflicti241 – 2411S → G AA sequence (PubMed:2026158).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXHX-ray1.22A/B/C/D2-254[»]
ProteinModelPortaliP19871.
SMRiP19871. Positions 2-254.
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: May 11, 2016
This is version 100 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.