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Database: UniProt
Entry: W5TI84_9NOCA
LinkDB: W5TI84_9NOCA
Original site: W5TI84_9NOCA 
ID   W5TI84_9NOCA            Unreviewed;       137 AA.
AC   W5TI84;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Putative methylmalonyl-CoA mutase small subunit {ECO:0000313|EMBL:AHH18942.1};
GN   ORFNames=NONO_c41580 {ECO:0000313|EMBL:AHH18942.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH18942.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH18942.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH18942.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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         Evidence={ECO:0000256|ARBA:ARBA00000290};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
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DR   EMBL; CP006850; AHH18942.1; -; Genomic_DNA.
DR   RefSeq; WP_025350358.1; NZ_CP006850.1.
DR   AlphaFoldDB; W5TI84; -.
DR   STRING; 1415166.NONO_c41580; -.
DR   KEGG; nno:NONO_c41580; -.
DR   PATRIC; fig|1415166.3.peg.4268; -.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_128233_0_0_11; -.
DR   OrthoDB; 9788468at2; -.
DR   Proteomes; UP000019150; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   PANTHER; PTHR48101:SF1; METHYLMALONYL-COA MUTASE, LARGE SUBUNIT; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT   DOMAIN          2..130
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   137 AA;  14083 MW;  CE111CD2D9CFA374 CRC64;
     MPARVLVAKP GLDGHDRGAK IVARTLRDAG FEVVYTGIRR RVEEIVSIAV AEDVAVVGLS
     ILSGAHLGLT AKVVAGLREA DAGDIAVVVG GTIPQADVPR LREAGAAAVF PTGTPLEELV
     TEIRALTGTT ALAPESR
//
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