UniProtKB - Q8HXX1 (MUTA_MACFA)
Protein
Methylmalonyl-CoA mutase, mitochondrial
Gene
MMUT
Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Functioni
Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.By similarity
Catalytic activityi
Cofactori
adenosylcob(III)alaminBy similarity
Activity regulationi
Inhibited by itaconyl-CoA, a metabolite that inactivates the coenzyme B12 cofactor.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 50 | malonyl-CoABy similarity | 1 | |
Binding sitei | 228 | malonyl-CoABy similarity | 1 | |
Binding sitei | 255 | malonyl-CoABy similarity | 1 | |
Binding sitei | 265 | malonyl-CoABy similarity | 1 | |
Metal bindingi | 627 | Cobalt (cobalamin 2 axial ligand)By similarity | 1 |
GO - Molecular functioni
- cobalamin binding Source: UniProtKB
- GTPase activity Source: UniProtKB
- identical protein binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- methylmalonyl-CoA mutase activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
Keywordsi
Molecular function | Isomerase |
Ligand | Cobalamin, Cobalt, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.2By similarity)Short name: MCM Alternative name(s): Methylmalonyl-CoA isomerase |
Gene namesi | Name:MMUT Synonyms:MUT ORF Names:QnpA-10043 |
Organismi | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
Taxonomic identifieri | 9541 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Proteomesi |
|
Subcellular locationi
Mitochondrion
- Mitochondrion matrix By similarity
- Mitochondrion By similarity
Other locations
- Cytoplasm By similarity
Mitochondrion
- mitochondrial matrix Source: UniProtKB
- mitochondrion Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, MitochondrionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 32 | MitochondrionSequence analysisAdd BLAST | 32 | |
ChainiPRO_0000019294 | 33 – 750 | Methylmalonyl-CoA mutase, mitochondrialAdd BLAST | 718 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 89 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 212 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 335 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 343 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 481 | PhosphoserineBy similarity | 1 | |
Modified residuei | 595 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 602 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinInteractioni
Subunit structurei
Homodimer.
Interacts (the apoenzyme form) with MMAA; the interaction is GTP dependent.
By similarityGO - Molecular functioni
- identical protein binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 9541.XP_005552835.1 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 614 – 746 | B12-bindingPROSITE-ProRule annotationAdd BLAST | 133 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 96 – 99 | malonyl-CoA bindingBy similarity | 4 | |
Regioni | 106 – 110 | malonyl-CoA bindingBy similarity | 5 | |
Regioni | 216 – 218 | malonyl-CoA bindingBy similarity | 3 | |
Regioni | 304 – 306 | malonyl-CoA bindingBy similarity | 3 |
Sequence similaritiesi
Belongs to the methylmalonyl-CoA mutase family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | ENOG502QQ7X, Eukaryota |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR006098, MMCoA_mutase_a_cat |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit TIGR00641, acid_CoA_mut_N, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit PS00544, METMALONYL_COA_MUTASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q8HXX1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLRVKNQLFL LSPHYLKQVK ESSGSRLIRQ RFLHQQQPLH PEWAALAKRQ
60 70 80 90 100
LKGKNPEDLI WHTPEGISIK PLYSKRDTTD LPEELPGVKP FTRGPYPTMY
110 120 130 140 150
TFRPWTIRQY AGFSTVEESN KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN
160 170 180 190 200
PRVRGDVGMA GVAIDTVEDT KILFDGIPLE KMSVSMTMNG AVIPVLANFI
210 220 230 240 250
VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK IIADIFQYTS
260 270 280 290 300
KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE
310 320 330 340 350
FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK SSKSLLLRAH
360 370 380 390 400
CQTSGWSLTE QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK
410 420 430 440 450
SARIARNTQI IIQEESGIPK VADPWGGSYM MESLTNDVYD AALKLINEIE
460 470 480 490 500
EMGGMAKAVA EGIPKLRIEE CAARRQARID SGSEVIVGVN KYQLEKEDAV
510 520 530 540 550
EVLAIDNTSV RNRQIEKLQK IKSSRDQALA ERCLAALTEC AASGDGNILA
560 570 580 590 600
LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA
610 620 630 640 650
IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL
660 670 680 690 700
FQTPREVAQQ AVDADVHAVG VSTLAAGHKT LVPELIKELN SLGRPDILVM
710 720 730 740 750
CGGVIPPQDY EFLFEVGVSN VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB083319 mRNA Translation: BAC20598.1 |
RefSeqi | NP_001306462.1, NM_001319533.1 |
Genome annotation databases
GeneIDi | 102131105 |
KEGGi | mcf:102131105 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB083319 mRNA Translation: BAC20598.1 |
RefSeqi | NP_001306462.1, NM_001319533.1 |
3D structure databases
SMRi | Q8HXX1 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9541.XP_005552835.1 |
Genome annotation databases
GeneIDi | 102131105 |
KEGGi | mcf:102131105 |
Organism-specific databases
CTDi | 4594 |
Phylogenomic databases
eggNOGi | ENOG502QQ7X, Eukaryota |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR006098, MMCoA_mutase_a_cat |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit TIGR00641, acid_CoA_mut_N, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit PS00544, METMALONYL_COA_MUTASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MUTA_MACFA | |
Accessioni | Q8HXX1Primary (citable) accession number: Q8HXX1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 12, 2005 |
Last sequence update: | March 1, 2003 | |
Last modified: | February 10, 2021 | |
This is version 85 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families