MUTA_BOVIN
ID MUTA_BOVIN Reviewed; 750 AA.
AC Q9GK13;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Methylmalonyl-CoA mutase, mitochondrial;
DE Short=MCM;
DE EC=5.4.99.2 {ECO:0000250|UniProtKB:P22033};
DE AltName: Full=Methylmalonyl-CoA isomerase;
DE Flags: Precursor;
GN Name=MMUT; Synonyms=MCM, MUT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Buckel T.;
RL Thesis (1998), University of Karlsruhe, Germany.
CC -!- FUNCTION: Catalyzes the reversible isomerization of methylmalonyl-CoA
CC (MMCoA) (generated from branched-chain amino acid metabolism and
CC degradation of dietary odd chain fatty acids and cholesterol) to
CC succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the
CC tricarboxylic acid cycle. {ECO:0000250|UniProtKB:P22033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC Evidence={ECO:0000250|UniProtKB:P22033};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889;
CC Evidence={ECO:0000250|UniProtKB:P22033};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250|UniProtKB:P22033};
CC -!- ACTIVITY REGULATION: Inhibited by itaconyl-CoA, a metabolite that
CC inactivates the coenzyme B12 cofactor. {ECO:0000250|UniProtKB:P22033}.
CC -!- SUBUNIT: Homodimer. Interacts (the apoenzyme form) with MMAA; the
CC interaction is GTP dependent. {ECO:0000250|UniProtKB:P22033}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P22033}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22033}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22033}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; AJ300476; CAC17595.1; -; mRNA.
DR AlphaFoldDB; Q9GK13; -.
DR SMR; Q9GK13; -.
DR STRING; 9913.ENSBTAP00000018963; -.
DR PaxDb; Q9GK13; -.
DR PeptideAtlas; Q9GK13; -.
DR PRIDE; Q9GK13; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR InParanoid; Q9GK13; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031419; F:cobalamin binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cobalamin; Cobalt; Cytoplasm; Isomerase; Metal-binding;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..750
FT /note="Methylmalonyl-CoA mutase, mitochondrial"
FT /id="PRO_5000066791"
FT DOMAIN 614..746
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 50
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 96..99
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 106..110
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 216..218
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 228
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 255
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 265
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 304..306
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT BINDING 627
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
FT MOD_RES 343
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22033"
FT MOD_RES 595
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
FT MOD_RES 602
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16332"
SQ SEQUENCE 750 AA; 83235 MW; 2E210F15408320A3 CRC64;
MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ LKGKNPEDLI
WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRLRGDVGMA GVAIDTVEDT KILFDGIPLE
KMSVSMTMNG AVIPVLATFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
IIADIFQYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT IADGLEYCRT GLQAGLTIDE
FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMLQPK NSKSLLLRAH CQTSGWSLTE
QDPYNNIIRT TIEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
VADPWGGSYM MESLTNDIYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
SGSEVIVGVN KYQLEKEESV DVLAIDNTSV RNKQIEKLKK VKSSRDQALA ERCLDALTAC
AASGDGNILA LAVDATRARC TVGEITYAMK KVFGEHKAND RMVSGAYRQE FGESKEIAFA
IKRVEKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ
AVDADVHTVG VSTLAAGHKT LVPELIKELN ALGRPDILVM CGGVIPPQDY EFLFEVGVSN
VFGPGTRIPK AAVQVLDDIE KCLEKKQQSI
