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Protein

Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial

Gene

CG15093

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.

Pathwayi: L-valine degradation

This protein is involved in the pathway L-valine degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-valine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211NAD; via amide nitrogenBy similarity
Active sitei196 – 1961By similarity
Binding sitei271 – 2711NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5830NADBy similarityAdd
BLAST
Nucleotide bindingi92 – 932NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-DME-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial (EC:1.1.1.31)
Short name:
HIBADH
Gene namesi
ORF Names:CG15093
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034390. CG15093.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionBy similarityAdd
BLAST
Chaini26 – 324299Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrialPRO_0000007161Add
BLAST

Proteomic databases

PaxDbiQ9V8M5.

Expressioni

Gene expression databases

BgeeiQ9V8M5.
GenevisibleiQ9V8M5. DM.

Interactioni

Protein-protein interaction databases

BioGridi62836. 1 interaction.
DIPiDIP-22109N.
IntActiQ9V8M5. 2 interactions.
MINTiMINT-1757357.
STRINGi7227.FBpp0085821.

Structurei

3D structure databases

ProteinModelPortaliQ9V8M5.
SMRiQ9V8M5. Positions 31-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0409. Eukaryota.
COG2084. LUCA.
GeneTreeiENSGT00530000063270.
InParanoidiQ9V8M5.
KOiK00020.
OMAiNIVHCGE.
OrthoDBiEOG7NSB31.
PhylomeDBiQ9V8M5.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9V8M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRVMSPAM LNAWSQTLVR AMSTQGGAKN IGFVGLGNMG ANMASNLIKA
60 70 80 90 100
GHKLHVFDIS KPACDGLAAK GATVYAKTSE LAKNSDFVIT MLPNNAIVDA
110 120 130 140 150
SYDEMTADGV NKDTIFIDSS TISPDLVKSL QKKISAKGAR FIDAPVSGGV
160 170 180 190 200
PGAEQATLTF MVGGTEAEYN AVKAVLECMG KKITHCGVYG MGQAAKLCNN
210 220 230 240 250
MMLAISMIGV SEAMNLAVRQ GLDANVFAEI INSSTGRCWA SEIYNPVPGV
260 270 280 290 300
CPSAPANRDY AGGFSSALIT KDLGLASGVA NASNSPIPLG SLAHKVYQSL
310 320
CDKGLGNKDF SVVYDLMKKE KFSV
Length:324
Mass (Da):33,883
Last modified:January 24, 2001 - v2
Checksum:iA39B534753EAE83E
GO

Sequence cautioni

The sequence AAL39202.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57639.2.
AY069057 mRNA. Translation: AAL39202.2. Different initiation.

Genome annotation databases

GeneIDi37166.
KEGGidme:Dmel_CG15093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57639.2.
AY069057 mRNA. Translation: AAL39202.2. Different initiation.

3D structure databases

ProteinModelPortaliQ9V8M5.
SMRiQ9V8M5. Positions 31-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62836. 1 interaction.
DIPiDIP-22109N.
IntActiQ9V8M5. 2 interactions.
MINTiMINT-1757357.
STRINGi7227.FBpp0085821.

Proteomic databases

PaxDbiQ9V8M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi37166.
KEGGidme:Dmel_CG15093.

Organism-specific databases

FlyBaseiFBgn0034390. CG15093.

Phylogenomic databases

eggNOGiKOG0409. Eukaryota.
COG2084. LUCA.
GeneTreeiENSGT00530000063270.
InParanoidiQ9V8M5.
KOiK00020.
OMAiNIVHCGE.
OrthoDBiEOG7NSB31.
PhylomeDBiQ9V8M5.

Enzyme and pathway databases

UniPathwayiUPA00362.
ReactomeiR-DME-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiCG15093. fly.
GenomeRNAii37166.
NextBioi802277.
PROiQ9V8M5.

Gene expression databases

BgeeiQ9V8M5.
GenevisibleiQ9V8M5. DM.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry namei3HIDH_DROME
AccessioniPrimary (citable) accession number: Q9V8M5
Secondary accession number(s): Q0E926, Q86R98, Q9V8M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: May 11, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.