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Q57307 (CHOD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 89. 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:
Cholesterol oxidase

EC=1.1.3.6
Alternative name(s):
Cholesterol isomerase
EC=5.3.3.1
Gene names
Name:choD
Ordered Locus Names:Rv3409c, MT3517
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process. Required for virulence. Ref.4

Catalytic activity

Cholesterol + O2 = cholest-5-en-3-one + H2O2. Ref.4

A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid. Ref.4

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; steroid biosynthesis.

Disruption phenotype

Cells lacking this gene show attenuated pathogenicity in peritoneal macrophages. Ref.4

Sequence similarities

Belongs to the GMC oxidoreductase family. Highly divergent.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Cholesterol oxidase
PRO_0000405326

Regions

Nucleotide binding11 – 2717FAD By similarity

Sites

Active site4701 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57307 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E72695DF493397C5

FASTA57863,024
        10         20         30         40         50         60 
MKPDYDVLII GSGFGGSVTA LRLTEKGYRV GVLEAGRRFS DEEFAKTSWD LRKFLWAPRL 

        70         80         90        100        110        120 
GCYGIQRIHP LRNVMILAGA GVGGGSLNYA NTLYVPPEPF FADQQWSHIT DWRGELMPHY 

       130        140        150        160        170        180 
QQAQRMLGVV QNPTFTDADR IVKEVADEMG FGDTWVPTPV GVFFGPDGTK TPGKTVPDPY 

       190        200        210        220        230        240 
FGGAGPARTG CLECGCCMTG CRHGAKNTLV KNYLGLAESA GAQVIPMTTV KGFERRSDGL 

       250        260        270        280        290        300 
WEVRTVRTGS WLRRDRRTFT ATQLVLAAGT WGTQHLLFKM RDRGRLPGLS KRLGVLTRTN 

       310        320        330        340        350        360 
SESIVGAATL KVNPDLDLTH GVAITSSIHP TADTHIEPVR YGKGSNAMGL LQTLMTDGSG 

       370        380        390        400        410        420 
PQGTDVPRWR QLLQTASQDP RGTIRMLNPR QWSERTVIAL VMQHLDNSIT TFTKRGKLGI 

       430        440        450        460        470        480 
RWYSSKQGHG EPNPTWIPIG NQVTRRIAAK IDGVAGGTWG ELFNIPLTAH FLGGAVIGDD 

       490        500        510        520        530        540 
PEHGVIDPYH RVYGYPTLYV VDGAAISANL GVNPSLSIAA QAERAASLWP NKGETDRRPP 

       550        560        570 
QGEPYRRLAP IQPAHPVVPA DAPGALRWLP IDPVSNAG 

« Hide

References

« Hide 'large scale' references
[1]"M.tuberculosis cholesterol oxidase."
Av-Gay Y., Lim W., Davies J.E.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[4]"Cholesterol oxidase is required for virulence of Mycobacterium tuberculosis."
Brzostek A., Dziadek B., Rumijowska-Galewicz A., Pawelczyk J., Dziadek J.
FEMS Microbiol. Lett. 275:106-112(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CHOLESTEROL DEGRADATION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK47855.1.
X99343 Genomic DNA. Translation: CAA67723.1.
AL123456 Genomic DNA. Translation: CCP46231.1.
PIRF70736.
RefSeqNP_217926.1. NC_000962.3.
NP_338041.1. NC_002755.2.
YP_006516895.1. NC_018143.1.

3D structure databases

ProteinModelPortalQ57307.
SMRQ57307. Positions 6-38, 472-524.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3409c.

Proteomic databases

PRIDEQ57307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47855; AAK47855; MT3517.
GeneID13317013.
887502.
922932.
KEGGmtc:MT3517.
mtu:Rv3409c.
PATRIC18129473. VBIMycTub22151_3832.

Organism-specific databases

TubercuListRv3409c.

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000241700.
KOK03333.
OMADPYHRVW.
ProtClustDBCLSK872179.

Enzyme and pathway databases

UniPathwayUPA00062.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF01266. DAO. 1 hit.
PF05199. GMC_oxred_C. 1 hit.
[Graphical view]
PROSITEPS00623. GMC_OXRED_1. False negative.
PS00624. GMC_OXRED_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHOD_MYCTU
AccessionPrimary (citable) accession number: Q57307
Secondary accession number(s): L0TFA8, Q799Z3, Q7D5K5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: November 1, 1996
Last modified: May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families