ID A0A2X0JD80_9ACTN Unreviewed; 681 AA.
AC A0A2X0JD80;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DN069_10740 {ECO:0000313|EMBL:RAG85588.1};
OS Streptacidiphilus pinicola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG85588.1, ECO:0000313|Proteomes:UP000248889};
RN [1] {ECO:0000313|EMBL:RAG85588.1, ECO:0000313|Proteomes:UP000248889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG85588.1,
RC ECO:0000313|Proteomes:UP000248889};
RA Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA Kim S.B.;
RT "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAG85588.1}.
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DR EMBL; QKYN01000039; RAG85588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0JD80; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000248889; Unassembled WGS sequence.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248889}.
FT DOMAIN 532..661
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 681 AA; 73227 MW; 1ED195DE870340CA CRC64;
MTVHRDRPWL MRTYAGHSSA AASNELYRKN LAKGQTGLSV AFDLPTQTGY NPDHVLARGE
VGRVGVPVSH VGDMRTLFEG IPLERTNTSM TINATAMWLL AMYQVVAEEQ GADIAKLTGT
TQNDIIKEYL SRGTHVFPPG PSIRLTTDMI AYTVANIPKW NPINICSYHL QEAGATPVQE
LAFAMCTAIA VLDAVRDSGQ VKPEQMGEVV ARISFFVNAG VRFVEEMCKL RAFAQLWEKV
TLERYGVTDP KQRRFRYGVQ VNSLGLTEAQ PENNVQRIVL EMLAVTLSKD ARARAVQLPA
WNEALGLPRP WDQQWSLRIQ QVLAFESDLL EYGDLFTGSV VVEAKVAELL AGAEAEIAKV
QEMGGAVAAV ESGYLKAALV ASHAERRARI ESGEDKVVGV NCYETTEPSP LTADLDTAIM
VVDGDAERAV AEAFTGWLAE RDEAAAQAAL GELKAQAATD ANLMTATLAC VRAGVTTGEW
AQALRDVFGE YRAPTGVGGA PITGTIDPES GSELLTVREA VARTAEELGS GKLRLLVGKP
GLDGHSNGAE QIAVRARDAG FEVVYQGIRL TPEQITAAAI AEDVHCVGLS ILSGAHAELV
PDVLQRLRRA GVEDMPVVVG GIIPAADEQA LLAQGVAAVF TPKDFGITAI IGRIVDEIRL
AHGLDPIFTT RKTQKEETLA S
//
