MUTB_STRCM
ID MUTB_STRCM Reviewed; 733 AA.
AC Q05065;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Methylmalonyl-CoA mutase large subunit;
DE EC=5.4.99.2;
DE AltName: Full=MCM-alpha;
GN Name=mutB;
OS Streptomyces cinnamonensis.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces virginiae group.
OX NCBI_TaxID=1900;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3823.5;
RX PubMed=8099072; DOI=10.1128/jb.175.11.3511-3519.1993;
RA Birch A., Leiser A., Robinson J.A.;
RT "Cloning, sequencing, and expression of the gene encoding methylmalonyl-
RT coenzyme A mutase from Streptomyces cinnamonensis.";
RL J. Bacteriol. 175:3511-3519(1993).
CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC CoA during synthesis of propionate from tricarboxylic acid-cycle
CC intermediates. This conversion most likely represents an important
CC source of building blocks for polyketide antibiotic biosynthesis. It is
CC unable to catalyze the conversion of isobutyryl-CoA into N-butyryl-CoA.
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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; L10064; AAA03041.1; -; Unassigned_DNA.
DR PIR; B40595; B40595.
DR AlphaFoldDB; Q05065; -.
DR SMR; Q05065; -.
DR PRIDE; Q05065; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
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 Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Metal-binding.
FT CHAIN 1..733
FT /note="Methylmalonyl-CoA mutase large subunit"
FT /id="PRO_0000194275"
FT DOMAIN 600..732
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 81
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 88
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 90
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 92
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 117
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 120
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 142
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 198
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 200
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 209
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 210
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 210
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 247
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 286
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 288
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 336
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 373
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 376
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 612
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 613
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 614
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 615
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 658
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 660
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 689
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 712
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT SITE 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P11653"
SQ SEQUENCE 733 AA; 79455 MW; F02EEB54A154FA59 CRC64;
MRIPEFDDIE LGAGGGPSGS AEQWRAAVKE SVGKSESDLL WETPEGIAVK PLYTGADVEG
LDFLETYPGV APYLRGPYPT MYVNQPWTIR QYAGFSTAEE SNAFYRRNLA AGQKGLSVAF
DLPTHRGYDS DHPRVTGDVG MAGVAIDSIY DMRQLFDGIP LDKMTVSMTM NGAVLPVLAL
YIVAAEEQGV PPEKLAGTIQ NDILKEFMVR NTYIYPPKPS MRIISDIFAY TSQKMPRYNS
ISISGYHIQE AGATADLELA YTLADGVEYL RAGQEAGLDV DAFAPRLSFF WAIGMNFFME
VAKLRAARLL WAKLVKQFDP KNAKSLSLRT HSQTSGWSLT AQDVFNNVTR TCVEAMAATQ
GHTQSLHTNA LDEALALPTD FSARIARNTQ LLIQQESGTT RTIDPWGGSA YVEKLTYDLA
RRAWQHIEEV EAAGGMAQAI DAGIPKLRVE EAAARTQARI DSGRQPVIGV NKYRVDTDEQ
IDVLKVDNSS VRAQQIEKLR RLREERDDAA CQDALRALTA AAERGPGQGL EGNLLALAVD
AARAKATVGE ISDALESVYG RHAGQIRTIS GVYRTEAGQS PSVERTRALV DAFDEAEGRR
PRILVAKMGQ DGHDRGQKVI ASAFADLGFD VDVGPLFQTP AEVARQAVEA DVHIVGVSSL
AAGHLTLVPA LREELAAEGR DDIMIVVGGV IPPQDVEALH EAGATAVFPP GTVIPDAAHD
LVKRLAADLG HEL
