MUTA_PONAB
ID MUTA_PONAB Reviewed; 750 AA.
AC Q5RFN2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=MUT;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857121; CAH89425.1; -; mRNA.
DR RefSeq; NP_001127145.1; NM_001133673.1.
DR AlphaFoldDB; Q5RFN2; -.
DR SMR; Q5RFN2; -.
DR STRING; 9601.ENSPPYP00000018666; -.
DR GeneID; 100174196; -.
DR KEGG; pon:100174196; -.
DR CTD; 4594; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR InParanoid; Q5RFN2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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 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:0000250"
FT CHAIN 33..750
FT /note="Methylmalonyl-CoA mutase, mitochondrial"
FT /id="PRO_0000324096"
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; 83122 MW; BE55177BF8807302 CRC64;
MLRAKNQLFL LSPHYLKQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ LKGKNPEDLI
WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRVRGDVGMA GVAIDTVEDT KILFDGIPLE
KMSVSMTMNG AVIPVLANFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
IIADIFEYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE
FAPRLSFFWG IGMNFYMEIT KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH CQTSGWSLTE
QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
VADPWGGSYM MECLTNDVYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
SGSEVIVGVN KYQLEKEDAV EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC
AASGDGNILA LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA
IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ
AVDADVHAVG VSTLAAGHKT LVPELIKELN SLGRPDILVM CGGVIPPQDY EFLFEVGVSN
VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV
