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Protein

3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase

Gene
N/A
Organism
Streptomyces exfoliatus (Streptomyces hydrogenans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Androstan-3-alpha,17-beta-diol + NAD+ = 17-beta-hydroxyandrostan-3-one + NADH.

Pathwayi: C21-steroid hormone metabolism

This protein is involved in the pathway C21-steroid hormone metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway C21-steroid hormone metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei139SubstrateBy similarity1
Active sitei152Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 34NADAdd BLAST25

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

UniPathwayiUPA00229.

Names & Taxonomyi

Protein namesi
Recommended name:
3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase (EC:1.1.1.53)
OrganismiStreptomyces exfoliatus (Streptomyces hydrogenans)
Taxonomic identifieri1905 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3243917.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000547131 – 2553-alpha-(or 20-beta)-hydroxysteroid dehydrogenaseAdd BLAST255

Proteomic databases

PRIDEiP19992.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Turni13 – 15Combined sources3
Helixi17 – 28Combined sources12
Beta strandi32 – 38Combined sources7
Helixi40 – 48Combined sources9
Helixi49 – 53Combined sources5
Beta strandi54 – 58Combined sources5
Helixi64 – 78Combined sources15
Beta strandi83 – 86Combined sources4
Helixi96 – 98Combined sources3
Helixi101 – 111Combined sources11
Helixi113 – 129Combined sources17
Beta strandi132 – 137Combined sources6
Helixi140 – 142Combined sources3
Helixi150 – 170Combined sources21
Helixi171 – 173Combined sources3
Beta strandi175 – 182Combined sources8
Helixi188 – 193Combined sources6
Helixi214 – 225Combined sources12
Helixi227 – 229Combined sources3
Beta strandi236 – 240Combined sources5
Turni241 – 245Combined sources5
Helixi249 – 253Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HDCX-ray2.20A/B/C/D2-255[»]
2HSDX-ray2.64A/B/C/D2-255[»]
ProteinModelPortaliP19992.
SMRiP19992.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19992.

Family & Domainsi

Sequence similaritiesi

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]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19992-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDLSGKTVI ITGGARGLGA EAARQAVAAG ARVVLADVLD EEGAATAREL
60 70 80 90 100
GDAARYQHLD VTIEEDWQRV VAYAREEFGS VDGLVNNAGI STGMFLETES
110 120 130 140 150
VERFRKVVDI NLTGVFIGMK TVIPAMKDAG GGSIVNISSA AGLMGLALTS
160 170 180 190 200
SYGASKWGVR GLSKLAAVEL GTDRIRVNSV HPGMTYTPMT AETGIRQGEG
210 220 230 240 250
NYPNTPMGRV GNEPGEIAGA VVKLLSDTSS YVTGAELAVD GGWTTGPTVK

YVMGQ
Length:255
Mass (Da):26,484
Last modified:February 1, 1991 - v1
Checksum:i9CB93CB66AA628D5
GO

Sequence databases

PIRiS10707.

Cross-referencesi

Sequence databases

PIRiS10707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HDCX-ray2.20A/B/C/D2-255[»]
2HSDX-ray2.64A/B/C/D2-255[»]
ProteinModelPortaliP19992.
SMRiP19992.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL3243917.

Proteomic databases

PRIDEiP19992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00229.

Miscellaneous databases

EvolutionaryTraceiP19992.

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]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSD_STREX
AccessioniPrimary (citable) accession number: P19992
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 94 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.