MUTA_MYCTU
ID MUTA_MYCTU Reviewed; 615 AA.
AC P9WJK7; L0T9S6; P65485; P71773;
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 small subunit;
DE Short=MCM;
DE EC=5.4.99.2;
GN Name=mutA; OrderedLocusNames=Rv1492; ORFNames=MTCY277.14;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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 -!- 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. {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44253.1; -; Genomic_DNA.
DR PIR; G70711; G70711.
DR RefSeq; NP_216008.1; NC_000962.3.
DR RefSeq; WP_003407585.1; NZ_NVQJ01000004.1.
DR PDB; 6OXC; X-ray; 1.90 A; B=1-615.
DR PDB; 6OXD; X-ray; 2.00 A; B=1-615.
DR PDBsum; 6OXC; -.
DR PDBsum; 6OXD; -.
DR AlphaFoldDB; P9WJK7; -.
DR SMR; P9WJK7; -.
DR STRING; 83332.Rv1492; -.
DR PaxDb; P9WJK7; -.
DR DNASU; 886507; -.
DR GeneID; 45425472; -.
DR GeneID; 886507; -.
DR KEGG; mtu:Rv1492; -.
DR TubercuList; Rv1492; -.
DR eggNOG; COG1884; Bacteria.
DR OMA; WYVERLT; -.
DR PhylomeDB; P9WJK7; -.
DR UniPathway; UPA00945; UER00910.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IBA:GO_Central.
DR GO; GO:0019652; P:lactate fermentation to propionate and acetate; IEA:InterPro.
DR GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IMP:MTBBASE.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR004608; MMCoA_mutase_b.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR00642; mmCoA_mut_beta; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin; Cobalt; Isomerase; Reference proteome.
FT CHAIN 1..615
FT /note="Probable methylmalonyl-CoA mutase small subunit"
FT /id="PRO_0000194265"
FT HELIX 12..27
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 232..252
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 274..295
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 321..335
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 390..412
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 420..439
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 473..489
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 503..519
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:6OXC"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 535..541
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 554..570
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:6OXC"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:6OXC"
FT HELIX 602..612
FT /evidence="ECO:0007829|PDB:6OXC"
SQ SEQUENCE 615 AA; 64744 MW; 82D52807A14BDA75 CRC64;
MSIDVPERAD LEQVRGRWRN AVAGVLSKSN RTDSAQLGDH PERLLDTQTA DGFAIRALYT
AFDELPEPPL PGQWPFVRGG DPLRDVHSGW KVAEAFPANG ATADTNAAVL AALGEGVSAL
LIRVGESGVA PDRLTALLSG VYLNLAPVIL DAGADYRPAC DVMLALVAQL DPGQRDTLSI
DLGADPLTAS LRDRPAPPIE EVVAVASRAA GERGLRAITV DGPAFHNLGA TAATELAATV
AAAVAYLRVL TESGLVVSDA LRQISFRLAA DDDQFMTLAK MRALRQLWAR VAEVVGDPGG
GAAVVHAETS LPMMTQRDPW VNMLRCTLAA FGAGVGGADT VLVHPFDVAI PGGFPGTAAG
FARRIARNTQ LLLLEESHVG RVLDPAGGSW FVEELTDRLA RRAWQRFQAI EARGGFVEAH
DFLAGQIAEC AARRADDIAH RRLAITGVNE YPNLGEPALP PGDPTSPVRR YAAGFEALRD
RSDHHLARTG ARPRVLLLPL GPLAEHNIRT TFATNLLASG GIEAIDPGTV DAGTVGNAVA
DAGSPSVAVI CGTDARYRDE VADIVQAARA AGVSRVYLAG PEKALGDAAH RPDEFLTAKI
NVVQALSNLL TRLGA
