ID A0A091JA79_EGRGA Unreviewed; 747 AA.
AC A0A091JA79;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE Flags: Fragment;
GN ORFNames=Z169_05207 {ECO:0000313|EMBL:KFP16630.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP16630.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP16630.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP16630.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: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; KK501614; KFP16630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JA79; -.
DR STRING; 188379.A0A091JA79; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
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:UP000053119}.
FT DOMAIN 612..744
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT NON_TER 747
FT /evidence="ECO:0000313|EMBL:KFP16630.1"
SQ SEQUENCE 747 AA; 82431 MW; 58029BECE5ACD262 CRC64;
MLRAKDALLR LRPCRCACLA QLPAGRLAWR SLHGQPLHPE WAALAEKQLK GKNPKDLIWH
TPEGINIKPL YSKRDTKDLP EELPGVKPFT RGPYPTMYTY RPWTIRQYAG FSTVEESNKF
YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM
SVSMTMNGAV IPVLATFIVT GEEQGVPQAK LTGTIQNDIL KEFMVRNTYI FPPEPSMRII
ADIFQYTSKH MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL KAGLTIDEFA
PRLSFFWGIG MNFYMEIAKL RAGRRLWAHL VEKMFKPKDP KSLLLRAHCQ TSGWSLTEQD
PFNNVIRTTI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA RIARNTQIII QEESGIPKVA
DPWGGSYLME CLTNDVYEAA LKLVEEIEEM GGMAKAVAEG IPKLRIEECA ARRQARIDSG
SEVIVGVNKH QLEKEETVEV LAIDNTSVRS KQIEKINKVK ASRDQAAAQQ CLAALTQCAA
TGEGNLLALA VEAARSRCTV GEITDAMKKV FGEHKASDRM VSGAYRQEFG ESDEILHAIN
RVNKFMDREG RRPRILVAKM GQDGHDRGAK VIATGFADIG FDVDIGPLFQ TPREVAQQAV
DADVHCVGVS TLAAGHKTLV PELIKELNAL GRPDILVICG GVIPPQDYDF LYEAGVTNVF
GPGTRIPKAA VQVLDDIEKC LEKRQQS
//
