Q59327 (OASD_COMTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 3-oxo-5-alpha-steroid 4-dehydrogenase EC=1.3.99.5 Alternative name(s): Delta 4, 5-alpha steroid dehydrogenase
Organism	Comamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier	285 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A. Ref.1
Catalytic activity	A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-Delta(4)-steroid + reduced acceptor. Ref.1 5-alpha-androstane-3,17-dione + acceptor = 5-alpha-4-androstene-3,17-dione + reduced acceptor. Ref.1 5-alpha-1-androstene-3,17-dione + acceptor = 1,4-androstadiene-3,17-dione + reduced acceptor. Ref.1
Cofactor	FAD Probable. Ref.1
Enzyme regulation	Inhibition occurrs with substrate concentrations above 25 µM. Ref.1
Subcellular location	Membrane; Single-pass membrane protein Potential Ref.1 Ref.2.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family.
Biophysicochemical properties	Kinetic parameters: KM=6.6 µM for 5-alpha-1-androstene-3,17-dione (at 30 degrees Celsius and at pH 8.2) Ref.1 KM=16.1 µM for 5-alpha-androstane-3,17-dione (at 30 degrees Celsius and at pH 8.2) Vmax=456 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as substrate (at 30 degrees Celsius and at pH 8.2) Vmax=700 nmol/min/mg enzyme with 5-alpha-1-androstene-3,17-dione as substrate (at 30 degrees Celsius and at pH 8.2) pH dependence: Optimum pH is 8. Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	FAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	steroid catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from electronic annotation. Source: EC 3-oxosteroid 1-dehydrogenase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 530	530	3-oxo-5-alpha-steroid 4-dehydrogenase		PRO_0000418533
Regions
	Transmembrane	395 – 415	21	Helical; Potential
	Nucleotide binding	33 – 62	30	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59327 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5E5D6CEAC0BF2EC1	FASTA	530	57,289
	10 20 30 40 50 60 MSNVKKHVST INPVGEVLDV GSADEVQWSD ASDVVVVGWG GAGASAAIEA REQGAEVLVI 70 80 90 100 110 120 ERFSGGGASV LSGGVVYAGA VPATRRKPAS RFTEAMTAYL KHEVNGVVSD ETLARFSRDS 130 140 150 160 170 180 VTNLNWLEKQ GATFASTMPG YKTSYPADGM YLYYSGNEVV PAYGNPQLLK KPPPRGHRVV 190 200 210 220 230 240 AKGQSGAMFF AALQKSTLAH GARTLTQARV QRLVREKDSG RVLGVEVMVL PEGDPRTERH 250 260 270 280 290 300 KKLDELVAKS ACIRRRVPRR VAVNVRRSRA RSARSATSVP AKVWCCPLAA ISSIRNCWSM 310 320 330 340 350 360 RRYKPGWLTG AAGCDGSGLR LGQSVGGIAQ DLNNISAWRF ITPPSVWPKG LVVNIQGERF 370 380 390 400 410 420 CNEQVYGAKL GYEMMEKQGG QAWLIIDSNV RRQAAWQCLF GGLWAFQSMP ALALMYKVAI 430 440 450 460 470 480 KGKSVDDLAK KLRMDAAVLQ LQFDRANAPA RGEIEDPLGK SQDMRHEFKG GSLFAIDISI 490 500 510 520 530 SQKMFPLAVL SLGGLKVNED NGAVIDGAGY DIPGLYAAGV PPLVWLPRVT

References

[1]

"Comamonas testosteroni 3-ketosteroid-delta 4(5 alpha)-dehydrogenase: gene and protein characterization." Florin C., Kohler T., Grandguillot M., Plesiat P. J. Bacteriol. 178:3322-3330(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, COFACTOR, SUBSTRATE SPECIFICITY.

[2]

"Bacterial oxidation of steroids. II. Studies on the enzymatic mechanism of ring A dehydrogenation." Levy H.R., Talalay P. J. Biol. Chem. 234:2014-2021(1959) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L23428 Genomic DNA. Translation: AAB08517.1.
PIR	JC6030.
3D structure databases
ProteinModelPortal	Q59327.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16925.
Family and domain databases
InterPro	IPR003953. FAD_bind_dom. [Graphical view]
Pfam	PF00890. FAD_binding_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OASD_COMTE

Accession

Primary (citable) accession number: Q59327

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program