ID A0A091V792_NIPNI Unreviewed; 746 AA.
AC A0A091V792;
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=Y956_03731 {ECO:0000313|EMBL:KFQ99206.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ99206.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ99206.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ99206.1};
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; KL410766; KFQ99206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091V792; -.
DR STRING; 128390.A0A091V792; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR Proteomes; UP000053283; 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:UP000053283}.
FT DOMAIN 611..743
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT NON_TER 746
FT /evidence="ECO:0000313|EMBL:KFQ99206.1"
SQ SEQUENCE 746 AA; 82535 MW; BA396EC81C56CB4F CRC64;
MLRAKDVLRL WPCRCTCLAQ LPACGLAWRL LHRQPLHPEW AALAEKQLKG KNPKDLIWHT
PEGIDIKPLY SKRDTKDLPE ELPGVKPFTR GPYPTMYTYR PWTIRQYAGF STVEESNKFY
KDNIKAGQQG LSVAFDLATH RGYDSDNPRV RGDVGMAGVA IDTVEDTKIL FDGIPLEKMS
VSMTMNGAVI PVLATFIVTG EEQGVPQAKL TGTIQNDILK EFMVRNTYIF PPEPSMRIIA
DIFQYTSKYM PKFNSISISG YHMQEAGADT ILELAYTIAD GLEYCRTGLK AGLTIDEFAP
RLSFFWGIGM NFYMEIAKLR AGRRLWAHLV EKMFKPKDPK SLLLRAHCQT SGWSLTEQDP
FNNVIRTTIE AMAAVFGGTQ SLHTNSFDEA LGLPTVKSAR IARNTQIIIQ EESGIPKVAD
PWGGSYLMEC LTNDVYEAAL KLVEEIEEMG GMAKAVAEGI PKLRIEECAA RRQARIDSGS
EVIVGVNKHQ LEKEETVEVL AIDNTSVRSK QIEKINKVKA SRDQAAAQQC LAALTQCAAT
GEGNLLALAV EAARSRCTVG EITDAMKKVF GEHKASDRMV SGAYRQEFGE SDEILHAINR
VNKFMDREGR RPRILVAKMG QDGHDRGAKV IATGFADIGF DVDIGPLFQT PREVAQQAVD
ADVHCVGVST LAAGHKTLVP ELIKELNALG RPDILVICGG VIPPQDYDFL YEAGVTNVFG
PGTRIPKAAV QVLDDIEKCL EKRQQS
//
