MUTB_MYCTU
ID MUTB_MYCTU Reviewed; 750 AA.
AC P9WJK5; 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 43.
DE RecName: Full=Probable methylmalonyl-CoA mutase large subunit;
DE Short=MCM;
DE EC=5.4.99.2;
GN Name=mutB; OrderedLocusNames=Rv1493; ORFNames=MTCY277.15;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44254.1; -; Genomic_DNA.
DR PIR; H70711; H70711.
DR RefSeq; NP_216009.1; NC_000962.3.
DR RefSeq; WP_003407587.1; NZ_NVQJ01000004.1.
DR PDB; 6OXC; X-ray; 1.90 A; A=1-750.
DR PDB; 6OXD; X-ray; 2.00 A; A=1-750.
DR PDBsum; 6OXC; -.
DR PDBsum; 6OXD; -.
DR AlphaFoldDB; P9WJK5; -.
DR SMR; P9WJK5; -.
DR STRING; 83332.Rv1493; -.
DR PaxDb; P9WJK5; -.
DR DNASU; 886509; -.
DR GeneID; 45425473; -.
DR GeneID; 886509; -.
DR KEGG; mtu:Rv1493; -.
DR TubercuList; Rv1493; -.
DR eggNOG; COG2185; Bacteria.
DR OMA; PWGGSAY; -.
DR PhylomeDB; P9WJK5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IBA:GO_Central.
DR GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cobalamin; Cobalt; Isomerase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..750
FT /note="Probable methylmalonyl-CoA mutase large subunit"
FT /id="PRO_0000194270"
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"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6OXD"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 230..247
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6OXD"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 268..288
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6OXD"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 384..388
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 423..445
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 449..455
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 457..474
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 503..518
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 521..535
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 550..559
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 564..575
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 588..593
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 597..613
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 618..622
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 631..643
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 656..666
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 680..694
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 712..718
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 720..724
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 730..745
FT /evidence="ECO:0007829|PDB:6OXC"
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
