ID M3WVH2_FELCA Unreviewed; 762 AA.
AC M3WVH2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Methylmalonyl-CoA mutase, mitochondrial {ECO:0000256|ARBA:ARBA00014305};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
DE AltName: Full=Methylmalonyl-CoA isomerase {ECO:0000256|ARBA:ARBA00033108};
GN Name=MMUT {ECO:0000313|Ensembl:ENSFCAP00000018359.2,
GN ECO:0000313|VGNC:VGNC:68362};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000018359.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000018359.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018359.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000018359.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018359.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000018359.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018359.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023743}.
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:0000256|ARBA:ARBA00023703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889;
CC Evidence={ECO:0000256|ARBA:ARBA00023703};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; AANG04003966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3WVH2; -.
DR PaxDb; 9685-ENSFCAP00000018359; -.
DR Ensembl; ENSFCAT00000022678.3; ENSFCAP00000018359.2; ENSFCAG00000025853.4.
DR VGNC; VGNC:68362; MMUT.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR GeneTree; ENSGT00390000011892; -.
DR HOGENOM; CLU_009523_3_1_1; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000025853; Expressed in adult mammalian kidney and 10 other cell types or tissues.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProt.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
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 NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 614..746
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 762 AA; 84439 MW; 9CB61B09A55684E7 CRC64;
MLRAKTWLLL LSPHHLKQLK ESSGSRLIWR RLLHQQQPLH PEWAALAKKQ LKGKNPEDLI
WHTPEGISIK PLYSSRDTND LPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRVRGDVGMA GVAIDTVEDT KILFDGIPLE
KMSVSMTMNG AVIPVLATFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
IIADIFQYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT IADGLEYCRT GLQAGLTIDE
FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH CQTSGWSLTE
QDPYNNIIRT TVEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
VADPWGGSYM MESLTNDVYD AALKLIHEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
SGSEVIVGVN KYQLEKEESV DVLAIDNTSV RNKQIEKLKK VKSSRDETLA ERCLVALTAC
AASGDGNILA LAVDAARARC TVGEITDAMK KVFGEHKAND RMVSGAYRQE FGESKEISFA
IQRVHKFMEL EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ
AVDADVHAVG VSTLAAGHKT LVPELIRELN SLGRPDILVM CGGVIPPQDY EFLFEVGVSS
VFGPGTRIPK AAVQVLGDIE KCLEKKQKSV SDNVGLQSQE LW
//
