MUTB_MYCTO
ID MUTB_MYCTO Reviewed; 750 AA.
AC P9WJK4; L0T9K4; P65487; P71774;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Probable methylmalonyl-CoA mutase large subunit;
DE Short=MCM;
DE EC=5.4.99.2;
GN Name=mutB; OrderedLocusNames=MT1540;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-
CC CoA during synthesis of propionate from tricarboxylic acid-cycle
CC intermediates. {ECO:0000250}.
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 Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45807.1; -; Genomic_DNA.
DR PIR; H70711; H70711.
DR RefSeq; WP_003407587.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJK4; -.
DR SMR; P9WJK4; -.
DR EnsemblBacteria; AAK45807; AAK45807; MT1540.
DR GeneID; 45425473; -.
DR KEGG; mtc:MT1540; -.
DR PATRIC; fig|83331.31.peg.1657; -.
DR HOGENOM; CLU_009523_3_1_11; -.
DR Proteomes; UP000001020; Chromosome.
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..750
FT /note="Probable methylmalonyl-CoA mutase large subunit"
FT /id="PRO_0000427814"
FT DOMAIN 616..748
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 91
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 94
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 101
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 103
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 105
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 130
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 133
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 155
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 211
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 213
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 222
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 223
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 223
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 260
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 299
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 301
FT /ligand="(R)-methylmalonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57326"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 349
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 386
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 389
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 628
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 629
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 630
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 631
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 674
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 676
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 705
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT BINDING 728
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250|UniProtKB:P11653"
FT SITE 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P11653"
SQ SEQUENCE 750 AA; 80604 MW; 9E6B866CE507D022 CRC64;
MTTKTPVIGS FAGVPLHSER AAQSPTEAAV HTHVAAAAAA HGYTPEQLVW HTPEGIDVTP
VYIAADRAAA EAEGYPLHSF PGEPPFVRGP YPTMYVNQPW TIRQYAGFST AADSNAFYRR
NLAAGQKGLS VAFDLATHRG YDSDHPRVQG DVGMAGVAID SILDMRQLFD GIDLSTVSVS
MTMNGAVLPI LALYVVAAEE QGVAPEQLAG TIQNDILKEF MVRNTYIYPP KPSMRIISDI
FAYTSAKMPK FNSISISGYH IQEAGATADL ELAYTLADGV DYIRAGLNAG LDIDSFAPRL
SFFWGIGMNF FMEVAKLRAG RLLWSELVAQ FAPKSAKSLS LRTHSQTSGW SLTAQDVFNN
VARTCIEAMA ATQGHTQSLH TNALDEALAL PTDFSARIAR NTQLVLQQES GTTRPIDPWG
GSYYVEWLTH RLARRARAHI AEVAEHGGMA QAISDGIPKL RIEEAAARTQ ARIDSGQQPV
VGVNKYQVPE DHEIEVLKVE NSRVRAEQLA KLQRLRAGRD EPAVRAALAE LTRAAAEQGR
AGADGLGNNL LALAIDAARA QATVGEISEA LEKVYGRHRA EIRTISGVYR DEVGKAPNIA
AATELVEKFA EADGRRPRIL IAKMGQDGHD RGQKVIATAF ADIGFDVDVG SLFSTPEEVA
RQAADNDVHV IGVSSLAAGH LTLVPALRDA LAQVGRPDIM IVVGGVIPPG DFDELYAAGA
TAIFPPGTVI ADAAIDLLHR LAERLGYTLD
