O18404 (HCD2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxyacyl-CoA dehydrogenase type-2
EC=1.1.1.35

Alternative name(s):
3-hydroxy-2-methylbutyryl-CoA dehydrogenase
EC=1.1.1.178
3-hydroxyacyl-CoA dehydrogenase type II
Mitochondrial ribonuclease P protein 2
Short name=Mitochondrial RNase P protein 2
Scully protein
Type II HADH

Gene names

Name:	scu
ORF Names:	CG7113

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function in mitochondrial tRNA maturation By similarity. May play a role in germline formation. Ref.1
Catalytic activity	(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.
Subunit structure	Multimer Potential.
Subcellular location	Mitochondrion By similarity.
Tissue specificity	Found in many tissues including CNS. Highest expression in both embryonic gonadal primordia and mature ovaries and testes. Ref.1
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Mitochondrion
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acyl-CoA metabolic process Inferred from direct assay PubMed 12917011. Source: FlyBase androgen metabolic process Inferred from direct assay PubMed 12917011. Source: FlyBase ecdysone metabolic process Inferred from direct assay PubMed 12917011. Source: FlyBase estrogen metabolic process Inferred from direct assay PubMed 12917011. Source: FlyBase fatty acid metabolic process Inferred from direct assay PubMed 12917011. Source: FlyBase tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Non-traceable author statement PubMed 12917011. Source: FlyBase lipid particle Inferred from direct assay PubMed 16543254PubMed 16979555. Source: FlyBase microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 7-beta-hydroxysteroid dehydrogenase (NADP+) activity Inferred from direct assay PubMed 12917011. Source: FlyBase acetoacetyl-CoA reductase activity Inferred from direct assay PubMed 12917011. Source: FlyBase estradiol 17-beta-dehydrogenase activity Inferred from direct assay PubMed 12917011. Source: FlyBase nucleotide binding Inferred from electronic annotation. Source: InterPro testosterone 17-beta-dehydrogenase (NAD+) activity Inferred from direct assay PubMed 12917011. Source: FlyBase testosterone dehydrogenase (NAD+) activity Inferred from direct assay PubMed 12917011. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 255	255	3-hydroxyacyl-CoA dehydrogenase type-2		PRO_0000054813
Regions
	Nucleotide binding	6 – 31	26	NAD By similarity
Sites
	Active site	162	1	Proton acceptor By similarity
	Binding site	149	1	Substrate By similarity
Experimental info
	Mutagenesis	33	1	L → Q: Lethal allele. Ref.1
	Mutagenesis	120	1	F → I: Lethal allele. Ref.1
	Sequence conflict	134	1	E → K in AAM51999. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O18404 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F58690643FA0FD03	FASTA	255	26,905
	10 20 30 40 50 60 MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD KVVFVPVDVT 70 80 90 100 110 120 SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN VAHRLEDFQR VININTVGTF 130 140 150 160 170 180 NVIRLSAGLM GANEPNQDGQ RGVIVNTASV AAFDGQIGQA AYSASKAAVV GMTLPIARDL 190 200 210 220 230 240 STQGIRICTI APGLFNTPML AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL 250 NGEVIRIDGA LRMMP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta peptide-binding protein." Torroja L., Ortuno-Sahagun D., Ferrus A., Haemmerle B., Barbas J.A. J. Cell Biol. 141:1009-1018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LEU-33 AND PHE-120. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y15102 mRNA. Translation: CAA75377.1. AE014298 Genomic DNA. Translation: AAF48797.1. AY121672 mRNA. Translation: AAM51999.1. BT029045 mRNA. Translation: ABJ16978.1.
RefSeq	NP_523396.1. NM_078672.4.
UniGene	Dm.7957.
3D structure databases
ProteinModelPortal	O18404.
SMR	O18404. Positions 2-255.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17092N.
IntAct	O18404. 2 interactions.
MINT	MINT-289527.
Proteomic databases
PaxDb	O18404.
PRIDE	O18404.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0074511; FBpp0074285; FBgn0021765.
GeneID	32789.
KEGG	dme:Dmel_CG7113.
Organism-specific databases
CTD	32789.
FlyBase	FBgn0021765. scu.
Phylogenomic databases
eggNOG	COG1028.
GeneTree	ENSGT00700000104319.
InParanoid	O18404.
KO	K08683.
OMA	HIFENDM.
OrthoDB	EOG4CVDPW.
PhylomeDB	O18404.
Gene expression databases
Bgee	O18404.
GermOnline	CG7113. Drosophila melanogaster.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	scu. drosophila.
GenomeRNAi	32789.
NextBio	780387.

Entry information

Entry name

HCD2_DROME

Accession

Primary (citable) accession number: O18404
Secondary accession number(s): Q059C3, Q8MRC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project