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UniProtKB/Swiss-Prot entry P69166

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HSD_MYCBO
Primary accession number P69166
Secondary accession number Q10855
Integrated into Swiss-Prot on February 15, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 22)
Name and origin of the protein
Protein name 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase
Synonym EC 1.1.1.53
Gene name
Name: fabG3
OrderedLocusNames: Mb2025
From
Mycobacterium bovis [TaxID: 1765] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-935 / AF2122/97;
DOI=10.1073/pnas.1130426100; PubMed=12788972 [NCBI, ExPASy, EBI, Israel, Japan]
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
"The complete genome sequence of Mycobacterium bovis.";
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
Comments
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
BX248341; CAD96878.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_855675.1; -.
3D structure databases
SMR P69166; 2-245.
ModBase P69166.
Ontologies
GO
GO:0047044; Molecular function: 3-alpha(or 20-beta)-hydroxysteroid dehydrogenase activity (inferred from electronic annotation from EC).
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.
BLOCKS P69166.
ProtoNet P69166.
Genome annotation databases
GeneID 1093793; -.
GenomeReviews BX248333_GR; Mb2025.
KEGG mbo:Mb2025; -.
Phylogenomic databases
HOGENOM P69166; -.
Genome annotation databases
CMR P69166; Mb2025.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Lipid metabolism; NAD; Oxidoreductase; Steroid metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   260  260     3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase. PRO_0000054711
NP_BIND   11    35  25     NAD (By similarity). 
ACT_SITE   153   153        Proton acceptor (By similarity). 
BINDING   140   140        Substrate (By similarity). 
Sequence information
Length: 260 AA [This is the length of the unprocessed precursor] Molecular weight: 27030 Da [This is the MW of the unprocessed precursor] CRC64: 0935A14ED36220B7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSGRLIGKVA LVSGGARGMG ASHVRAMVAE GAKVVFGDIL DEEGKAVAAE LADAARYVHL 

        70         80         90        100        110        120 
DVTQPAQWTA AVDTAVTAFG GLHVLVNNAG ILNIGTIEDY ALTEWQRILD VNLTGVFLGI 

       130        140        150        160        170        180 
RAVVKPMKEA GRGSIINISS IEGLAGTVAC HGYTATKFAV RGLTKSTALE LGPSGIRVNS 

       190        200        210        220        230        240 
IHPGLVKTPM TDWVPEDIFQ TALGRAAEPV EVSNLVVYLA SDESSYSTGA EFVVDGGTVA 

       250        260 
GLAHNDFGAV EVSSQPEWVT
P69166 in FASTA format

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