MUTA_PROFR
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 03-AUG-2022, entry version 142.
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; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC 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}.
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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 PDBsum; 1E1C; -.
DR PDBsum; 1REQ; -.
DR PDBsum; 2REQ; -.
DR PDBsum; 3REQ; -.
DR PDBsum; 4REQ; -.
DR PDBsum; 5REQ; -.
DR PDBsum; 6REQ; -.
DR PDBsum; 7REQ; -.
DR AlphaFoldDB; P11652; -.
DR SMR; P11652; -.
DR DIP; DIP-6149N; -.
DR IntAct; P11652; 1.
DR MINT; P11652; -.
DR BioCyc; MetaCyc:MON-13076; -.
DR BRENDA; 5.4.99.2; 5032.
DR SABIO-RK; P11652; -.
DR UniPathway; UPA00945; UER00910.
DR EvolutionaryTrace; P11652; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0019652; P:lactate fermentation to propionate and acetate; IEA:InterPro.
DR Gene3D; 1.10.196.20; -; 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; 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; 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..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1REQ"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3REQ"
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 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 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 461..463
FT /evidence="ECO:0007829|PDB:1REQ"
FT STRAND 464..466
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 571..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
