ID MUTA_STRCM Reviewed; 616 AA. AC Q05064; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=Methylmalonyl-CoA mutase small subunit; DE EC=5.4.99.2; DE AltName: Full=MCM-beta; GN Name=mutA; OS Streptomyces cinnamonensis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1900; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A3823.5; RX MEDLINE=93273720; PubMed=8099072; RA Birch A., Leiser A., Robinson J.A.; RT "Cloning, sequencing, and expression of the gene encoding RT methylmalonyl-coenzyme A mutase from Streptomyces cinnamonensis."; RL J. Bacteriol. 175:3511-3519(1993). CC -!- FUNCTION: Catalyzes the isomerization of succinyl-CoA to CC methylmalonyl-CoA during synthesis of propionate from CC tricarboxylic acid-cycle intermediates. This conversion most CC likely represents an important source of building blocks for CC polyketide antibiotic biosynthesis. It is unable to catalyze the CC conversion of isobutyryl-CoA into N-butyryl-CoA. CC -!- CATALYTIC ACTIVITY: (R)-methylmalonyl-CoA = succinyl-CoA. CC -!- COFACTOR: Adenosylcobalamin. CC -!- PATHWAY: Metabolic intermediate metabolism; propionyl-CoA CC degradation; succinyl-CoA from propionyl-CoA: step 3/3. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L10064; AAA03040.1; -; Unassigned_DNA. DR PIR; A40595; A40595. DR HSSP; P11652; 2REQ. DR BRENDA; 5.4.99.2; 1647. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW. DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:EC. DR GO; GO:0019652; P:lactate fermentation to propionate and acetate; IEA:InterPro. DR InterPro; IPR014348; Cbl-dep_enz_cat-sub. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006099; MMCoA_mutase_a/b_cat. DR InterPro; IPR004608; MMCoA_mutase_b. DR Gene3D; G3DSA:3.40.50.280; B12_bd; 1. DR Gene3D; G3DSA:3.20.20.240; Cobalamin-dep_enz_cat; 1. DR Pfam; PF01642; MM_CoA_mutase; 1. DR TIGRFAMs; TIGR00642; mmCoA_mut_beta; 1. DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1. PE 3: Inferred from homology; KW Cobalamin; Cobalt; Isomerase. FT CHAIN 1 616 Methylmalonyl-CoA mutase small subunit. FT /FTId=PRO_0000194269. SQ SEQUENCE 616 AA; 65041 MW; 09CA24006E169AE6 CRC64; MTVLPDDGLS LAAEFPDATH EQWHRLVEGV VRKSGKDVSG TAAEEALSTT LEDGLTTRPL YTARDAAPDA GFPGFAPFVR GSVPEGNTPG GWDVRQRYAS ADPARTNEAV LTDLENGVTS LWLTLGSAGL PVTGLERALD GVYLDLVPVA LDAGSEAATA ARELLRLYEA AGVADDAVRG TLGADPLGHE ARTGEKSTSF AAVAELARLC GERYPGLRAL TVDALPYHEA GASAAQELGA SLATGVEYLR ALHDKGLGVE KAFAQLEFRF AATADQFLTI AKLRAARRLW ARVAEVSGVP AAGAQRQHAV TSPVMMTRRD PWVNMLRTTV ACLGAGVGGA DAVTVLPFDH ELGLPDAFAR RIARNTSTIL LEESHLARVI DPAGGSWYVE RLTDELAHAA WDFFKEIERA DGQVAALRSG LVGDRIAATW AERRKKLARR REPITGVSEF PLLTERPVER EPAPAAPPGG LPRVRRDEAY EELRGRSDAH LEATGARPKV FIAALGPAAA HTARATFAAN LFMAGGVEPV HDPVSVDAET AAEAFAASGA TVACLCSSDV LYAEQAEAVA RALKSAGALR VFLAGRGEFA DIDEYVFAGC DAVAVLTSTL DRMGVA //