ID I4BIZ6_MYCCN Unreviewed; 761 AA.
AC I4BIZ6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=Mycch_2480 {ECO:0000313|EMBL:AFM17253.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM17253.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM17253.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM17253.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC CoA during synthesis of propionate from tricarboxylic acid-cycle
CC intermediates. {ECO:0000256|ARBA:ARBA00003359}.
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:ARBA00000290};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; CP003053; AFM17253.1; -; Genomic_DNA.
DR RefSeq; WP_014815733.1; NC_018027.1.
DR AlphaFoldDB; I4BIZ6; -.
DR STRING; 710421.Mycch_2480; -.
DR KEGG; mcb:Mycch_2480; -.
DR PATRIC; fig|710421.3.peg.2477; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_11; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000006057; Chromosome.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AFM17253.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 627..759
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT COILED 516..543
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 761 AA; 81143 MW; 24419C864B7AEBD0 CRC64;
MTVHDVAGQP APATKPSMID SFADVPLDGG AAAATPSAGD VAAQLSAAAA AHGYSADQLD
WSTPEGIDVK PVYIAADRDE VAGAGYPLDS LPGEPPFVRG PYPTMYVNQP WTIRQYAGFS
TAAESNAFYR RNLAAGQKGL SVAFDLATHR GYDSDHPRVA GDVGMAGVAI DSILDMRQLF
DGIDLSSVSV SMTMNGAVLP ILALYVVAAE EQGVPPEKLA GTIQNDILKE FMVRNTYIYP
PKPSMRIISD IFGYTSAKMP KFNSISISGY HIQEAGATAD LELGYTLADG VEYIKAGLDA
GLDIDKFAPR LSFFWGIGMN FFMEVAKLRA GRLLWSELVS QFDPKNPKSL SLRTHSQTSG
WSLTAQDAFN NVARTCVEAM AATQGHTQSL HTNALDEALA LPTDFSARIA RNTQLLLQQE
SGTTRSIDPW GGSYYVEWLT YQLAEKARAH IREIAEHGGM AQAINEGIPK LRIEEAAART
QARIDSGAQT VIGVNRYQVD EDHEIEVLKV ENSRVRAEQI AKLERLRSER DDAATQAALA
ELTRAAAASG TAGHDGLGNN LLALAIDAAR AKATVGEISD ALEKVYGRHQ AEIRTISGVY
RDEVGMAGNV SSATELVEKF AEADGRRPRI LVAKMGQDGH DRGQKVIATA FADIGFDVDV
GSLFSTPEEV ARQAADNDVH VVGVSSLAAG HLTLVPALRD ALADVGRPDI MIVVGGVIPP
GDFDELYAAG ATAIFPPGTV IADAAIGLLH KLAERLGYPL S
//
