ID L5JLK2_PTEAL Unreviewed; 739 AA.
AC L5JLK2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=PAL_GLEAN10025342 {ECO:0000313|EMBL:ELK00225.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00225.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB031158; ELK00225.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JLK2; -.
DR STRING; 9402.L5JLK2; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR InParanoid; L5JLK2; -.
DR Proteomes; UP000010552; 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:UP000010552}.
FT DOMAIN 603..735
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 739 AA; 81923 MW; C9CEA40BAC71422F CRC64;
MLRAKTRLFL LSPHHLKQLK ESSVSRVLWQ RLLHQQQPLH PEWAVLAKKQ LKGKNPEDLI
WRTPEGISIK PLYSSRDTKD LPEELPGVEP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN
RFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRVRGDVGMA GVAIDTVEDT KILFDGIPLE
KMSVSMTMNG AVIPVLANFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK
IIADIFQYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT IADGLEYCRT GLQAGLTIDE
FAPRLSFFWG IGMNFYMEIA KMRAGRKLWA HLIEKIFQPK NSKSLLLRAH CQTSGWSLTE
QDPYNNIIRT TIEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK
VADPWGGSYM MESLTNDVYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID
SGSEVIVGVN KYQLEQEEPV DVMMIDNTSV KSSRDQALAE RCLAALTECA ASGDGNILAL
AVDAARARCT VGEITDAMKK VFGEHKANDR MVSGAYRQEF GESKEISFAI KRVHKFMERE
GRRPRLLVAK MGQDGHDRGA KVIATGFADL GFDVDIGPLF QTPLEVAQQA VDADVHAVGV
STLAAGHKTL VPELIKQLNS LGRPDILVMC GGVIPPQDYE FLLEVGVSNI FGPGTRIPKA
AVQVLDDIEK CLEKKQQSM
//
