P12676 (CHOD_STRS0) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cholesterol oxidase
Short name=CHOD
EC=1.1.3.6

Alternative name(s):
Cholesterol isomerase
EC=5.3.3.1

Gene names

Name:

choA

Organism

Streptomyces sp. (strain SA-COO)

Taxonomic identifier

74576 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
Catalytic activity	Cholesterol + O2 = cholest-5-en-3-one + H2O2. Ref.2 A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid. Ref.2
Cofactor	FAD.
Pathway	Steroid metabolism; cholesterol metabolism.
Subunit structure	Monomer.
Subcellular location	Secreted.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Sterol metabolism
Cellular component	Secreted
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Isomerase Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cholesterol oxidase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro steroid delta-isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 42

42

Tat-type signal

Chain

43 – 546

504

Cholesterol oxidase

PRO_0000012333

Regions

Nucleotide binding

54 – 70

17

FAD Potential

Sites

Active site

398

1

Proton acceptor

Active site

484

1

Experimental info

Mutagenesis

398

1

E → Q: Reduced activity.

Mutagenesis

484

1

H → N or Q: Reduced activity.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

546

Helix Strand Turn

Details...

Turn

42 – 44

3

Beta strand

47 – 53

7

Helix

57 – 68

12

Beta strand

73 – 79

7

Beta strand

89 – 92

4

Beta strand

95 – 97

3

Helix

100 – 102

3

Beta strand

103 – 105

3

Helix

116 – 119

4

Helix

120 – 122

3

Beta strand

132 – 137

6

Beta strand

142 – 146

5

Helix

151 – 154

4

Helix

165 – 171

7

Helix

177 – 182

6

Helix

184 – 192

9

Helix

199 – 204

6

Helix

206 – 208

3

Helix

209 – 220

12

Beta strand

225 – 227

3

Beta strand

230 – 232

3

Helix

234 – 241

8

Helix

249 – 251

3

Beta strand

259 – 262

4

Turn

265 – 268

4

Helix

269 – 275

7

Beta strand

278 – 292

15

Beta strand

296 – 305

10

Beta strand

311 – 324

14

Helix

327 – 340

14

Turn

349 – 352

4

Beta strand

361 – 366

6

Beta strand

383 – 387

5

Beta strand

395 – 400

6

Beta strand

410 – 417

8

Beta strand

425 – 428

4

Turn

429 – 432

4

Beta strand

433 – 436

4

Helix

440 – 443

4

Helix

444 – 461

18

Beta strand

468 – 473

6

Beta strand

476 – 478

3

Beta strand

480 – 484

5

Turn

491 – 493

3

Beta strand

499 – 501

3

Beta strand

505 – 509

5

Helix

512 – 514

3

Helix

524 – 542

19

Sequences

	Sequence		Length	Mass (Da)
	P12676 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: EF22A1FE5EA68D21	FASTA	546	58,994
	10 20 30 40 50 60 MTAQQHLSRR RMLGMAAFGA AALAGGTTIA APRAAAAAKS AADNGGYVPA VVIGTGYGAA 70 80 90 100 110 120 VSALRLGEAG VQTLMLEMGQ LWNQPGPDGN IFCGMLNPDK RSSWFKNRTE APLGSFLWLD 130 140 150 160 170 180 VVNRNIDPYA GVLDRVNYDQ MSVYVGRGVG GGSLVNGGMA VEPKRSYFEE ILPRVDSSEM 190 200 210 220 230 240 YDRYFPRANS MLRVNHIDTK WFEDTEWYKF ARVSREQAGK AGLGTVFVPN VYDFGYMQRE 250 260 270 280 290 300 AAGEVPKSAL ATEVIYGNNH GKQSLDKTYL AAALGTGKVT IQTLHQVKTI RQTKDGGYAL 310 320 330 340 350 360 TVEQKDTDGK LLATKEISCR YLFLGAGSLG STELLVRARD TGTLPNLNSE VGAGWGPNGN 370 380 390 400 410 420 IMTARANHMW NPTGAHQSSI PALGIDAWDN SDSSVFAEIA PMPAGLETWV SLYLAITKNP 430 440 450 460 470 480 QRGTFVYDAA TDRAKLNWTR DQNAPAVNAA KALFDRINKA NGTIYRYDLF GTQLKAFADD 490 500 510 520 530 540 FCYHPLGGCV LGKATDDYGR VAGYKNLYVT DGSLIPGSVG VNPFVTITAL AERNVERIIK QDVTAS

References

[1]	"Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp." Ishizaki T., Hirayama N., Shinkawa H., Nimi O., Murooka Y. J. Bacteriol. 171:596-601(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants." Yue Q.K., Kass I.J., Sampson N.S., Vrielink A. Biochemistry 38:4277-4286(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31939 Genomic DNA. Translation: AAA26719.1.

PIR

A32260.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B4V	X-ray	1.50	A	43-546	[»]
1B8S	X-ray	1.65	A	43-546	[»]
1CBO	X-ray	1.80	A	43-546	[»]
1CC2	X-ray	2.20	A	43-546	[»]
1IJH	X-ray	1.53	A	43-546	[»]
1MXT	X-ray	0.95	A	43-546	[»]
1N1P	X-ray	0.95	A	43-546	[»]
1N4U	X-ray	0.95	A	43-546	[»]
1N4V	X-ray	1.00	A	43-546	[»]
1N4W	X-ray	0.92	A	43-546	[»]
2GEW	X-ray	0.97	A	43-546	[»]
3B3R	X-ray	0.98	A	42-546	[»]
3B6D	X-ray	1.20	A	43-546	[»]
3CNJ	X-ray	0.95	A	45-543	[»]
3GYI	X-ray	1.00	A	43-546	[»]
3GYJ	X-ray	0.92	A	43-546	[»]

ProteinModelPortal

P12676.

SMR

P12676. Positions 45-545.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00296.

Family and domain databases

InterPro

IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
IPR006311. TAT_signal.
[Graphical view]

Pfam

PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]

PROSITE

PS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. False negative.
PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12676.

Entry information

Entry name

CHOD_STRS0

Accession

Primary (citable) accession number: P12676

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program