Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Gene

l(2)04524

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism (By similarity). Vital for adult survival.By similarity

Catalytic activityi

ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.

Pathwayi: L-leucine degradation

This protein is involved in step 2 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (l(2)04524)
  3. no protein annotated in this organism
This subpathway is part of the pathway L-leucine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA, the pathway L-leucine degradation and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

  • leucine catabolic process Source: UniProtKB-UniPathway
  • leucine metabolic process Source: FlyBase
  • regulation of eclosion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-196780. Biotin transport and metabolism.
R-DME-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00363; UER00861.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.4)
Short name:
MCCase subunit beta
Alternative name(s):
3-methylcrotonyl-CoA carboxylase 2
3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:l(2)04524
ORF Names:CG3267
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0042083. CG3267.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 578549Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000000297Add
BLAST

Proteomic databases

PaxDbiQ9V9A7.
PRIDEiQ9V9A7.

Expressioni

Tissue specificityi

Expressed in third instar larval ring gland (lateral and medial secretory cells and corpus cardiacum cells) and CNS.1 Publication

Gene expression databases

BgeeiQ9V9A7.
ExpressionAtlasiQ9V9A7. differential.
GenevisibleiQ9V9A7. DM.

Interactioni

Protein-protein interaction databases

BioGridi72857. 1 interaction.
STRINGi7227.FBpp0085460.

Structurei

3D structure databases

ProteinModelPortaliQ9V9A7.
SMRiQ9V9A7. Positions 29-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 572519CarboxyltransferaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 38834Acyl-CoA bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000142812.
InParanoidiQ9V9A7.
KOiK01969.
OMAiQCIVVAN.
OrthoDBiEOG77M8NF.
PhylomeDBiQ9V9A7.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9V9A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRLNWLFRS SSVLLRSQVR LLHVGDANVL HSEVDKQSAE YKENAREMAS
60 70 80 90 100
LVGDLRNFTS QVLKGGGQKA IERHTSRGKL LARERINLLL DKGSPFLELS
110 120 130 140 150
ALAGHELYGE EVVNSGGIVT GVGRVCGTEC LVVANDATVK GGSYYPITVK
160 170 180 190 200
KHLRAQEIAQ ENRLPCIYLV DSGGANLPRQ ADVFPDKLHF GRIFYNQANM
210 220 230 240 250
SAQGIPQIAV VMGSCTAGGA YVPAMADESI IVKKQGTIFL AGPPLVKAAT
260 270 280 290 300
GEEVSAEDLG GADLHCKTSG VTDHYALDDE HALYLARQIV SNLNLSATNS
310 320 330 340 350
YNDQLMHSSQ VNFQTATPPS AVEEPRYDAE ELYGIVGPNL TKSFDVREVI
360 370 380 390 400
ARIVDGSRFT EFKKLYGETL VCGFAKLYGH TVGIVGNNGV LFSESALKGA
410 420 430 440 450
HFIQLCAQRK IPLVFLQNIT GFMVGRDAEA NGIAKNGAKM VTAVACANVP
460 470 480 490 500
KFTVIIGGSY GAGNYGMCGR AYSPRFLYMW PNSRISVMGG TQAANVMAQI
510 520 530 540 550
TEDQRKRAGK EFSEEEAQKL KAPIVEMFEA EGSPYYSTAR LWDDGIIDPA
560 570
NTRQILGLSL KAALNNAGQE TKFGVFRM
Length:578
Mass (Da):62,648
Last modified:May 1, 2000 - v1
Checksum:iAF5E2ABBE36B18F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501S → R no nucleotide entry (PubMed:9584098).Curated
Sequence conflicti96 – 961F → G no nucleotide entry (PubMed:9584098).Curated
Sequence conflicti274 – 2741H → N in AAL89883 (PubMed:12537569).Curated
Sequence conflicti277 – 2771L → V no nucleotide entry (PubMed:9584098).Curated
Sequence conflicti330 – 3301E → R no nucleotide entry (PubMed:9584098).Curated
Sequence conflicti376 – 3772KL → NV no nucleotide entry (PubMed:9584098).Curated
Sequence conflicti422 – 4221Missing no nucleotide entry (PubMed:9584098).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM70824.1.
AF006654 mRNA. Translation: AAB62570.1.
AY084145 mRNA. Translation: AAL89883.1.
RefSeqiNP_652724.1. NM_144467.2.
UniGeneiDm.5216.

Genome annotation databases

EnsemblMetazoaiFBtr0086126; FBpp0085460; FBgn0042083.
GeneIDi59261.
KEGGidme:Dmel_CG3267.
UCSCiCG3267-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM70824.1.
AF006654 mRNA. Translation: AAB62570.1.
AY084145 mRNA. Translation: AAL89883.1.
RefSeqiNP_652724.1. NM_144467.2.
UniGeneiDm.5216.

3D structure databases

ProteinModelPortaliQ9V9A7.
SMRiQ9V9A7. Positions 29-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi72857. 1 interaction.
STRINGi7227.FBpp0085460.

Proteomic databases

PaxDbiQ9V9A7.
PRIDEiQ9V9A7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086126; FBpp0085460; FBgn0042083.
GeneIDi59261.
KEGGidme:Dmel_CG3267.
UCSCiCG3267-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0042083. CG3267.

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000142812.
InParanoidiQ9V9A7.
KOiK01969.
OMAiQCIVVAN.
OrthoDBiEOG77M8NF.
PhylomeDBiQ9V9A7.

Enzyme and pathway databases

UniPathwayiUPA00363; UER00861.
ReactomeiR-DME-196780. Biotin transport and metabolism.
R-DME-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiCG3267. fly.
GenomeRNAii59261.
NextBioi841761.
PROiQ9V9A7.

Gene expression databases

BgeeiQ9V9A7.
ExpressionAtlasiQ9V9A7. differential.
GenevisibleiQ9V9A7. DM.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 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: Embryo.
  4. "Genes expressed in the ring gland, the major endocrine organ of Drosophila melanogaster."
    Harvie P.D., Filippova M., Bryant P.J.
    Genetics 149:217-231(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-126 AND 271-578, TISSUE SPECIFICITY.
    Tissue: Larval CNS and Larval ring gland.

Entry informationi

Entry nameiMCCB_DROME
AccessioniPrimary (citable) accession number: Q9V9A7
Secondary accession number(s): O18364, Q8SXT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 110 of the entry and version 1 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.