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Database: UniProt
Entry: E6S6E3_INTC7
LinkDB: E6S6E3_INTC7
Original site: E6S6E3_INTC7 
ID   E6S6E3_INTC7            Unreviewed;       675 AA.
AC   E6S6E3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   OrderedLocusNames=Intca_2425 {ECO:0000313|EMBL:ADU48932.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS   12989 / 7 KIP).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU48932.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU48932.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA   Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
CC   -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC       {ECO:0000256|ARBA:ARBA00008465}.
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DR   EMBL; CP002343; ADU48932.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6S6E3; -.
DR   STRING; 710696.Intca_2425; -.
DR   KEGG; ica:Intca_2425; -.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_4_0_11; -.
DR   Proteomes; UP000008914; Chromosome.
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   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
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   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR   PANTHER; PTHR48101:SF3; COENZYME B12-DEPENDENT MUTASE; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADU48932.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT   DOMAIN          535..664
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   675 AA;  72472 MW;  07E6FE2E20FF7E9C CRC64;
     MRTYAGHSSA AASNALYRRN LAKGQTGLSV AFDLPTQTGY DPDHVLARGE VGKVGVPVSH
     IGDVEALFHD IPLRDMNTSM TINATAMWLL SLYQVAAERQ AEAAGESPEE WVHALAGTTQ
     NDIIKEYLSR GTYVFPPGPS LRLITDMIAY TVREIPKWNP INICSYHLQE AGATPVQEIA
     FSMSTAIAVL DAVRDSGQVP EDEFSEVVAR ISFFVNAGVR FVEEMCKMRA FVELWDRVTG
     ERYGVTDAKA RRFRYGVQVN SLGLTEAQPE NNVQRIVLEM LGVTLSKDAR ARALQLPAWN
     EALGLPRPWD QQWSLRMQQV LAFESDLLEY DDLFTGSVVV ERKVAQLVEG ASAEIARIEE
     MGGAVAAVES GYMKSALVAS HAERRRRIES GEEVIVGLNR FETTEPNPLT ADLGTAIQTV
     DPSVEKAASD AVRAWRDRRD ADPTRRDRAA AALARLKADA AAGTNLMAAS LECARAQVTT
     GEWAGALREQ FGEYRAPTGV SGSVGVASAE AGESGTGLGA VRAAVTRTSE ELGEKLRILV
     GKPGLDGHSN GAEQVAVRAR DAGFEVIYQG IRLTPQQIVA AAVAEDVHVV GLSILSGSHM
     ELVPEVIDGL RAAGAGDVPV IVGGIIPEGD AVQLRAAGVA MVFTPKDFGL NEIMGEIVGV
     VRASRGLGLL EHPRA
//
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