ID G1KMV1_ANOCA Unreviewed; 746 AA.
AC G1KMV1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:ENSACAP00000012593.2};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012593.2, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000012593.2, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012593.2,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000012593.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_003215418.1; XM_003215370.3.
DR AlphaFoldDB; G1KMV1; -.
DR STRING; 28377.ENSACAP00000012593; -.
DR Ensembl; ENSACAT00000012849.4; ENSACAP00000012593.2; ENSACAG00000012754.4.
DR GeneID; 100556169; -.
DR KEGG; acs:100556169; -.
DR CTD; 4594; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR GeneTree; ENSGT00390000011892; -.
DR HOGENOM; CLU_009523_3_1_1; -.
DR InParanoid; G1KMV1; -.
DR OMA; IQEETHI; -.
DR OrthoDB; 304517at2759; -.
DR TreeFam; TF313557; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000012754; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IBA:GO_Central.
DR GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0050667; P:homocysteine metabolic process; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
DR GO; GO:1901290; P:succinyl-CoA biosynthetic process; IEA:Ensembl.
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:UP000001646}.
FT DOMAIN 610..742
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 746 AA; 82600 MW; 4A64D790505AE524 CRC64;
MFRSKNGILR IWPFCYKKEA GSQHREHIQR SLHELHPGWA AMAKTQLKGK DPGELMWHTP
EGISIKPLYS ARDTKDLPEE LPGLKPFTRG PYPTMYTYRP WTIRQYAGFS TVEESNKFYK
DNIRAGQQGL SVAFDLATHR GYDSDNPRVR GDVGMAGVAI DTVEDTKILF DGIPLEKMSV
SMTMNGAVIP ILANFIVAGE EQGVPQSKLT GTIQNDILKE FMVRNTYIFP PEPSMRIIAD
IFQYTSKHMP KFNSISISGY HMQEAGADAI LELAYTVADG LEYCRTGLQA GLTIDEFAPR
LSFFWGIGMN FYMEIAKLRA GRRLWAHLIE RMFQPKDSKS LLLRAHCQTS GWSLTEQDPY
NNIIRTAIEA MAAVFGGTQS LHTNSFDEAL GLPTVKSARI ARNTQIIIQE ESGIPKVADP
WGGSFLMESL TNDVYEAALK LIDEIEEMGG MAKAVAEGIP KLRIEECAAR RQARIDSGSE
VIVGVNKYQL EKEETVEVLA IDNTSVRNKQ IEKLKRVKAS RDEAAAQSCL AALTDCAATS
QGNLLALAVE AARARCTVGE ITNAMKKVFG EHRASDRMVS GAYRQEFGES DEIVRVINRV
NTFMECEGRR PRLLVAKMGQ DGHDRGAKVI ATGFADLGFD VDISPLFQTP HEVAQQAVDA
DVHCVGVSTL AAGHKTLVPE LIKELSALGR PDILVMCGGV IPPQDYDFLY DSGVSNIFGP
GTRIPKAALQ VLDDIEKCLN KRQQLL
//
