ID MUTA_PROFR Reviewed; 638 AA. AC P11652; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 153. DE RecName: Full=Methylmalonyl-CoA mutase small subunit; DE EC=5.4.99.2; DE AltName: Full=MCB-beta; GN Name=mutA; OS Propionibacterium freudenreichii subsp. shermanii. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales; OC Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=1752; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 4-9; 96-100; RP 302-306; 473-478 AND 523-527. RC STRAIN=NCIMB 9885; RX PubMed=2569861; DOI=10.1042/bj2600345; RA Marsh E.N., McKie N., Davis N.K., Leadlay P.F.; RT "Cloning and structural characterization of the genes coding for RT adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium RT shermanii."; RL Biochem. J. 260:345-352(1989). RN [2] RP PROTEIN SEQUENCE OF 515-518. RC STRAIN=NCIMB 9885; RX PubMed=2569860; DOI=10.1042/bj2600339; RA Marsh E.N., Leadlay P.F.; RT "Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for RT the presence of two masked cysteine residues."; RL Biochem. J. 260:339-343(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=NCIMB 9885; RX PubMed=8805541; DOI=10.1016/s0969-2126(96)00037-8; RA Mancia F., Keep N.H., Nakagawa A., Leadlay P.F., McSweeney S., RA Rasmussen B., Bosecke P., Diat O., Evans P.R.; RT "How coenzyme B12 radicals are generated: the crystal structure of RT methylmalonyl-coenzyme A mutase at 2-A resolution."; RL Structure 4:339-350(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC STRAIN=NCIMB 9885; RX PubMed=9655823; DOI=10.1016/s0969-2126(98)00073-2; RA Mancia F., Evans P.R.; RT "Conformational changes on substrate binding to methylmalonyl CoA mutase RT and new insights into the free radical mechanism."; RL Structure 6:711-720(1998). CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl- CC CoA during synthesis of propionate from tricarboxylic acid-cycle CC intermediates. 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 -!- COFACTOR: CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation; CC succinyl-CoA from propanoyl-CoA: step 3/3. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC -!- INTERACTION: CC P11652; P11653: mutB; NbExp=4; IntAct=EBI-1027328, EBI-1027336; CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14965; CAA33089.1; -; Genomic_DNA. DR PIR; S04640; S04640. DR PDB; 1E1C; X-ray; 2.62 A; B/D=2-638. DR PDB; 1REQ; X-ray; 2.00 A; B/D=2-638. DR PDB; 2REQ; X-ray; 2.50 A; B/D=2-638. DR PDB; 3REQ; X-ray; 2.70 A; B=2-638. DR PDB; 4REQ; X-ray; 2.20 A; B/D=2-638. DR PDB; 5REQ; X-ray; 2.20 A; B/D=2-638. DR PDB; 6REQ; X-ray; 2.20 A; B/D=2-638. DR PDB; 7REQ; X-ray; 2.20 A; B/D=2-638. DR AlphaFoldDB; P11652; -. DR SMR; P11652; -. DR DIP; DIP-6149N; -. DR IntAct; P11652; 1. DR MINT; P11652; -. DR BioCyc; MetaCyc:MONOMER-13076; -. DR BRENDA; 5.4.99.2; 5032. DR SABIO-RK; P11652; -. DR UniPathway; UPA00945; UER00910. DR EvolutionaryTrace; P11652; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC. DR CDD; cd03677; MM_CoA_mutase_beta; 1. DR Gene3D; 1.10.196.20; -; 1. DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1. DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1. DR InterPro; IPR016176; Cbl-dep_enz_cat. DR InterPro; IPR036724; Cobalamin-bd_sf. DR InterPro; IPR024067; Me-malonyl-CoA_mutase_sm_su_N. DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat. DR InterPro; IPR058549; MeMalonylCoA_mutase_a/b_site. DR InterPro; IPR004608; MMCoA_mutase_b. DR NCBIfam; TIGR00642; mmCoA_mut_beta; 1. DR PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 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; PS00544; METMALONYL_COA_MUTASE; 1. DR PDBsum; 1E1C; -. DR PDBsum; 1REQ; -. DR PDBsum; 2REQ; -. DR PDBsum; 3REQ; -. DR PDBsum; 4REQ; -. DR PDBsum; 5REQ; -. DR PDBsum; 6REQ; -. DR PDBsum; 7REQ; -. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..638 FT /note="Methylmalonyl-CoA mutase small subunit" FT /id="PRO_0000194268" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..11 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:4REQ" FT HELIX 32..44 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:3REQ" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 55..62 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:4REQ" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 118..129 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:4REQ" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 201..208 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:2REQ" FT HELIX 217..223 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 248..268 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 273..277 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 280..286 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 290..311 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 319..321 FT /evidence="ECO:0007829|PDB:7REQ" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:2REQ" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 338..353 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 356..359 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 363..367 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 369..373 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 374..388 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 403..425 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 429..434 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 437..454 FT /evidence="ECO:0007829|PDB:1REQ" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 478..481 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 495..506 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 514..517 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 521..537 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 544..546 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 550..560 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 563..568 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 574..578 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 579..587 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 591..597 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 599..605 FT /evidence="ECO:0007829|PDB:1REQ" FT HELIX 606..612 FT /evidence="ECO:0007829|PDB:1REQ" FT STRAND 615..617 FT /evidence="ECO:0007829|PDB:4REQ" FT HELIX 623..633 FT /evidence="ECO:0007829|PDB:1REQ" SQ SEQUENCE 638 AA; 69464 MW; F44C708AA8D47075 CRC64; MSSTDQGTNP ADTDDLTPTT LSLAGDFPKA TEEQWEREVE KVLNRGRPPE KQLTFAECLK RLTVHTVDGI DIVPMYRPKD APKKLGYPGV APFTRGTTVR NGDMDAWDVR ALHEDPDEKF TRKAILEGLE RGVTSLLLRV DPDAIAPEHL DEVLSDVLLE MTKVEVFSRY DQGAAAEALV SVYERSDKPA KDLALNLGLD PIAFAALQGT EPDLTVLGDW VRRLAKFSPD SRAVTIDANI YHNAGAGDVA ELAWALATGA EYVRALVEQG FTATEAFDTI NFRVTATHDQ FLTIARLRAL REAWARIGEV FGVDEDKRGA RQNAITSWRD VTREDPYVNI LRGSIATFSA SVGGAESITT LPFTQALGLP EDDFPLRIAR NTGIVLAEEV NIGRVNDPAG GSYYVESLTR SLADAAWKEF QEVEKLGGMS KAVMTEHVTK VLDACNAERA KRLANRKQPI TAVSEFPMIG ARSIETKPFP AAPARKGLAW HRDSEVFEQL MDRSTSVSER PKVFLACLGT RRDFGGREGF SSPVWHIAGI DTPQVEGGTT AEIVEAFKKS GAQVADLCSS AKVYAQQGLE VAKALKAAGA KALYLSGAFK EFGDDAAEAE KLIDGRLFMG MDVVDTLSST LDILGVAK //