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Protein

Citramalyl-CoA lyase, mitochondrial

Gene

Clybl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial citramalyl-CoA lyase indirectly involved in the vitamin B12 metabolism (PubMed:29056341). Converts citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway (By similarity). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, a vitamin B12-poisoning metabolite (PubMed:29056341). Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate (By similarity). Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (By similarity). Also has very weak citramalate synthase activity in vitro (By similarity).By similarity1 Publication

Caution

This organism lacks the other subunits that are necessary for ATP-independent citrate lyase activity. Even though this protein has clear similarity to citrate lyase beta subunit, it is expected to have a somewhat different enzyme activity.Curated

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.By similarity
Propionyl-CoA + H2O + glyoxylate = beta-methylmalate + CoA.By similarity
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate.By similarity

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48SubstrateBy similarity1
Binding sitei55SubstrateBy similarity1
Binding sitei59SubstrateBy similarity1
Binding sitei105SubstrateBy similarity1
Metal bindingi169MagnesiumBy similarity1
Metal bindingi204MagnesiumBy similarity1
Active sitei318By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase, Transferase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.3.6 3474

Names & Taxonomyi

Protein namesi
Recommended name:
Citramalyl-CoA lyase, mitochondrial (EC:4.1.3.25By similarity)
Alternative name(s):
Beta-methylmalate synthase (EC:2.3.3.-By similarity)
Citrate lyase subunit beta-like protein, mitochondrial
Short name:
Citrate lyase beta-like
Malate synthase (EC:2.3.3.9By similarity)
Gene namesi
Name:ClyblImported
Synonyms:Clb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1916884 Clybl

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 20MitochondrionSequence analysisAdd BLAST20
ChainiPRO_000028639021 – 338Citramalyl-CoA lyase, mitochondrialAdd BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55N6-acetyllysineCombined sources1
Modified residuei59N6-acetyllysineCombined sources1
Modified residuei64N6-acetyllysineCombined sources1
Modified residuei80N6-acetyllysine; alternateCombined sources1
Modified residuei80N6-succinyllysine; alternateCombined sources1
Modified residuei90N6-acetyllysine; alternateCombined sources1
Modified residuei90N6-succinyllysine; alternateCombined sources1
Modified residuei307N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8R4N0
MaxQBiQ8R4N0
PaxDbiQ8R4N0
PeptideAtlasiQ8R4N0
PRIDEiQ8R4N0

2D gel databases

REPRODUCTION-2DPAGEiQ8R4N0

PTM databases

iPTMnetiQ8R4N0
PhosphoSitePlusiQ8R4N0

Expressioni

Tissue specificityi

Detected in brown fat, brain, liver, kidney, heart, skeletal muscle and ovary (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000025545 Expressed in 284 organ(s), highest expression level in brown adipose tissue
CleanExiMM_CLYBL
GenevisibleiQ8R4N0 MM

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

IntActiQ8R4N0, 1 interactor
MINTiQ8R4N0
STRINGi10090.ENSMUSP00000026625

Structurei

3D structure databases

ProteinModelPortaliQ8R4N0
SMRiQ8R4N0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni270 – 271Substrate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGUQ Eukaryota
COG2301 LUCA
GeneTreeiENSGT00390000017163
HOGENOMiHOG000242281
HOVERGENiHBG059382
InParanoidiQ8R4N0
KOiK11390
OMAiAWLFCPA
OrthoDBiEOG091G0EXW
PhylomeDBiQ8R4N0
TreeFamiTF313596

Family and domain databases

InterProiView protein in InterPro
IPR005000 Aldolase/citrate-lyase_domain
IPR011206 Citrate_lyase_beta/mcl1/mcl2
IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
PfamiView protein in Pfam
PF03328 HpcH_HpaI, 1 hit
PIRSFiPIRSF015582 Cit_lyase_B, 1 hit
SUPFAMiSSF51621 SSF51621, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8R4N0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALCVLRNTV RGAAALPRLK ASHVVSVYKP RYSSLSNHKY VPRRAVLYVP
60 70 80 90 100
GNDEKKIRKI PSLKVDCAVL DCEDGVAENK KNEARLRIAK TLEDFDLGTT
110 120 130 140 150
EKCVRINSVS SGLAEVDLET FLQARVLPSS LMLPKVEGPE EIRWFSDKFS
160 170 180 190 200
LHLKGRKLEQ PMNLIPFVET AMGLLNFKAV CEETLKTGPQ VGLCLDAVVF
210 220 230 240 250
GGEDFRASIG ATSNKDTQDI LYARQKVVVT AKAFGLQAID LVYIDFRDED
260 270 280 290 300
GLLRQSREAA AMGFTGKQVI HPNQIAVVQE QFTPTPEKIQ WAEELIAAFK
310 320 330
EHQQLGKGAF TFRGSMIDMP LLKQAQNIVT LATSIKEK
Length:338
Mass (Da):37,549
Last modified:May 1, 2007 - v2
Checksum:i6F8AA53D9EDC3958
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9T → A in AAL84704 (PubMed:11741334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428254 mRNA Translation: AAL84704.1
AK009345 mRNA Translation: BAB26232.1
BC023398 mRNA Translation: AAH23398.1
CCDSiCCDS27346.1
RefSeqiNP_083832.2, NM_029556.3
UniGeneiMm.34608

Genome annotation databases

EnsembliENSMUST00000026625; ENSMUSP00000026625; ENSMUSG00000025545
GeneIDi69634
KEGGimmu:69634
UCSCiuc007vax.2 mouse

Similar proteinsi

Entry informationi

Entry nameiCLYBL_MOUSE
AccessioniPrimary (citable) accession number: Q8R4N0
Secondary accession number(s): Q9D7D0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: September 12, 2018
This is version 109 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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