ID K0V7T1_MYCVA Unreviewed; 723 AA.
AC K0V7T1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
DE Flags: Fragment;
GN ORFNames=MVAC_19638 {ECO:0000313|EMBL:EJZ07089.1};
OS Mycolicibacterium vaccae ATCC 25954.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ07089.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ07089.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ07089.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL J. Bacteriol. 194:6339-6340(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJZ07089.1}.
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DR EMBL; ALQA01000047; EJZ07089.1; -; Genomic_DNA.
DR RefSeq; WP_003931982.1; NZ_JH814695.1.
DR AlphaFoldDB; K0V7T1; -.
DR PATRIC; fig|1194972.3.peg.3913; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_11; -.
DR Proteomes; UP000006072; 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 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:EJZ07089.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 589..721
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT COILED 478..505
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EJZ07089.1"
SQ SEQUENCE 723 AA; 77663 MW; A81CE95DE8E99B37 CRC64;
ADVDRQVSAA AAAHGYTADQ LDWSTPEGIE VKPVYIGADR DSIVEAGYPL NTLPGEPPFV
RGPYPTMYVN QPWTIRQYAG FSTAAESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDHPR
VAGDVGMAGV AIDSILDMRQ LFDGIDLSSV SVSMTMNGAV LPILALYVVA AEEQGVPPEK
LAGTIQNDIL KEFMVRNTYI YPPKPSMRII SDIFGYTSVK MPKFNSISIS GYHIQEAGAT
ADLELGYTLA DGVEYIKAGL DAGLDIDKFA PRLSFFWGIG MNFFMEVAKL RAGRLLWSEL
VSQFDPKSAK SLSLRTHSQT SGWSLTAQDA FNNVARTCVE AMAATQGHTQ SLHTNALDEA
LALPTDFSAR IARNTQLLLQ QESGTTRPID PWAGSYYVEW LTYQLAEKAR AHIAEIAEHG
GMAQAIDAGI PKLRIEEAAA RTQARIDSGQ QTVIGVNRYQ VDEDHEIEVL KVENSRVRAE
QIAKLERLRS QRDDAATQAA LAELTRAAAA SGPAGEDGLG NNLLALAINA ARAKATVGEI
SDALEKVYGR HQAEIRTIAG VYRDEVGMAS NVSSATELVE KFAEADGRRP RILVAKMGQD
GHDRGQKVIA TAFADIGFDV DVGSLFSTPE EVARQAADND VHVVGVSSLA AGHLTLVPAL
RDALAEVGRP DIMVVVGGVI PPGDFDELYE AGATAIFPPG TVIADAAIGL LNKLAERLGY
SLS
//
