Reviewed, UniProtKB/Swiss-Prot Q04616 (3O1D_RHOOP)

Names and origin

Protein names	Recommended name:     3-oxosteroid 1-dehydrogenase     EC=1.3.99.4
Organism	Rhodococcus opacus (Nocardia opaca)
Taxonomic identifier	37919 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	507 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	Dehydrogenates steroids by introducing a double bond in steroid ring A.
Catalytic activity	A 3-oxosteroid + acceptor = a 3-oxo-Delta(1)-steroid + reduced acceptor.
Cofactor	FAD.
Pathway	Lipid metabolism; steroid degradation.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Induction	By steroids.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxosteroid 1-dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 507	506	3-oxosteroid 1-dehydrogenase		PRO_0000064377
Regions
	Nucleotide binding	9 – 38	30	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04616-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 067F865E9E7ED984	FASTA	507	54,005
	10 20 30 40 50 60 MQDWTSECDL LVVGSGGGAL TGAYTAAAQG LTTIVLEKTD RFGGTSAYSG ASIWLPGTQV 70 80 90 100 110 120 QERAGLPDST ENARSYLRAL LGDAESERQD AYVETAPAVV ALLEQNPNIE FEFRAFPDYY 130 140 150 160 170 180 KAEGRMDTGR SINPLDLDPA DIGDLAGRCV RNCTKTDRMD HAPGRMIGGR ALIAVSAAVQ 190 200 210 220 230 240 STARQNFAPE SVLTSLIVED GRVVGGLRSN PRYRQRIKAN RGVLMHAGGG FEGNAEMREQ 250 260 270 280 290 300 AGTPGKAIWS MGPSGPTPAT RSPPELAGRR RNSLARSGVV LPRGRAARRR RLHGRVRGGL 310 320 330 340 350 360 VVDSPGSVPQ RVASVRPVRT SHGCSPDDNG SAVPSFMIFD SREVTDCPPS ASRTRPPPST 370 380 390 400 410 420 SKPEPGSVPT LSKNSLPRPD YRPERIAQHC RKVQRCRKLG VDEEFHRGED PYDAFFCPPN 430 440 450 460 470 480 GGANAALTAI ENGPFYAARD RLSDLGTKGG LVTDVNGRVL RADGSAIDGL YAAGNTSASV 490 500 APFYPGPGVP LGTAMVFSYR AAQDMAK

References

[1]	Drobnic K. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IMET 7030.
[2]	"Improved purification of steroid 1:2-dehydrogenase from Nocardia opaca and partial characterization of its cloned gene sequence." Drobnic K., Krizaj I., Gubensek F., Komel R. Biochem. Biophys. Res. Commun. 190:509-515(1993) [PubMed: 7916596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, PROTEIN SEQUENCE OF 2-15.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U59422 Genomic DNA. Translation: AAB02831.1.
PIR	PC1242.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.99.4. 2206.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

3O1D_RHOOP

Accession

Primary (citable) accession number: Q04616

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 51 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)