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P69167 (HSD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase

EC=1.1.1.53
Gene names
Name:fabG3
Ordered Locus Names:Rv2002, MT2058
ORF Names:MTCY39.16c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; C21-steroid hormone metabolism.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processLipid metabolism
Steroid metabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsteroid metabolic process

Inferred from direct assay Ref.3. Source: MTBBASE

   Cellular componentplasma membrane

Inferred from direct assay. Source: MTBBASE

   Molecular functionandrostan-3-alpha,17-beta-diol dehydrogenase activity

Inferred from direct assay Ref.3. Source: MTBBASE

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2602603-alpha-(or 20-beta)-hydroxysteroid dehydrogenase
PRO_0000054712

Regions

Nucleotide binding11 – 3525NAD By similarity

Sites

Active site1531Proton acceptor
Binding site1401Substrate

Experimental info

Sequence conflict1741S → G in AAK46335. Ref.2

Secondary structure

.............................................. 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69167 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 0935A14ED36220B7

FASTA26027,030
        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 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis."
Yang J.K., Park M.S., Waldo G.S., Suh S.W.
Proc. Natl. Acad. Sci. U.S.A. 100:455-460(2003) [PubMed: 12524453] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS THR-6; MET-47 AND LYS-69.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842578 Genomic DNA. Translation: CAA98414.1.
AE000516 Genomic DNA. Translation: AAK46335.1.
PIRH70758.
RefSeqNP_216518.1. NC_000962.2.
NP_336521.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NFFX-ray1.80A/B1-260[»]
1NFQX-ray2.40A/B/C/D1-260[»]
1NFRX-ray2.10A/B/C/D1-260[»]
ProteinModelPortalP69167.
SMRP69167. Positions 2-245.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001684; EBMYCP00000001684; EBMYCG00000001683.
EBMYCT00000072037; EBMYCP00000070096; EBMYCG00000072032.
GeneID888857.
923379.
GenomeReviewsGene locus MT2058 in contig AE000516_GR.
Gene locus Rv2002 in contig AL123456_GR.
KEGGmtc:MT2058.
mtu:Rv2002.
PATRIC18126286. VBIMycTub22151_2255.
TIGRMT2058.

Organism-specific databases

TubercuListRv2002.

Phylogenomic databases

GeneTreeEBGT00050000015165.
HOGENOMHBG750976.
OMAWQRILDI.
PhylomeDBP69167.
ProtClustDBCLSK871992.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00038.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHSD_MYCTU
AccessionPrimary (citable) accession number: P69167
Secondary accession number(s): Q10855
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families