ID A0A1H7LC23_STRJI Unreviewed; 681 AA.
AC A0A1H7LC23;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN05414137_104449 {ECO:0000313|EMBL:SEK96494.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=235985 {ECO:0000313|EMBL:SEK96494.1, ECO:0000313|Proteomes:UP000183015};
RN [1] {ECO:0000313|Proteomes:UP000183015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC / KCTC 19219 / NBRC 100920 / 33214
RC {ECO:0000313|Proteomes:UP000183015};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOAZ01000004; SEK96494.1; -; Genomic_DNA.
DR RefSeq; WP_075003844.1; NZ_FOAZ01000004.1.
DR AlphaFoldDB; A0A1H7LC23; -.
DR STRING; 235985.SAMN05414137_104449; -.
DR eggNOG; COG2185; Bacteria.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000183015; 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:UP000183015}.
FT DOMAIN 532..661
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 681 AA; 73112 MW; E205D50B9E431179 CRC64;
MTVHRDRPWL MRTYAGHSSA AASNELYRKN LAKGQTGLSV AFDLPTQTGY NPDHVLARGE
VGRVGVPVSH VGDMRTLFEG IPLERTNTSM TINATAMWLL AMYQVVAEEQ GADIAKLTGT
TQNDIIKEYL SRGTHVFPPG PSIRLTTDMI AYTVAHIPKW NPINICSYHL QEAGATPVQE
LAFAMCTAIA VLDAVRDSGQ VKPEQMGEVV ARISFFVNAG VRFVEEMCKL RAFAQLWEKV
TLERYGVTDP KQRRFRYGVQ VNSLGLTEAQ PENNVQRIVL EMLAVTLSKD ARARAVQLPA
WNEALGLPRP WDQQWSLRIQ QVLAFESDLL EYGDLFTGSV VVEAKVAELL AGAEAEIAKV
QEMGGAVAAV ESGYLKAALV ASHAERRGRI ESGEDKVVGV NCYETTEPSP LTADLDTAIM
VVDGDAERAV AEAFAGWLAA RDEAAAQAAL AELKAQAQTD ASLMTATLAC VRAGVTTGEW
SQALRDVFGE YRAPTGVGGA PITGVIDPDS GSELLTVREA VARTAQELGS GKLRLLVGKP
GLDGHSNGAE QIAVRARDAG FEVVYQGIRL TPEQITAAAI AEDVHCVGLS ILSGAHAELV
PDVLQRLRRA GAEDVPVVVG GIIPAADEQA LLAQGVAAVF TPKDFGITAI IGHIVDEIRL
AHGLDPIFTT RKTQKEETLA S
//
