ID A0A396SBM5_9BACI Unreviewed; 715 AA.
AC A0A396SBM5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=D1B33_05990 {ECO:0000313|EMBL:RHW38430.1};
OS Lysinibacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2304605 {ECO:0000313|EMBL:RHW38430.1, ECO:0000313|Proteomes:UP000265692};
RN [1] {ECO:0000313|EMBL:RHW38430.1, ECO:0000313|Proteomes:UP000265692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-03 {ECO:0000313|EMBL:RHW38430.1,
RC ECO:0000313|Proteomes:UP000265692};
RA Yu L.;
RT "Lysinibacillus sp. YLB-03 draft genome sequence.";
RL Submitted (AUG-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 -!- 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:RHW38430.1}.
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DR EMBL; QWEI01000002; RHW38430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396SBM5; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000265692; 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 CDD; cd03679; MM_CoA_mutase_alpha_like; 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:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 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:RHW38430.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265692}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 715 AA; 79444 MW; 114AC79163A8A879 CRC64;
MKPNFSSINI QEIMVNENLQ PKHNVETNEG IEVKEFYQSD DLQDVKHLND VPGVAPNTRG
PYPTMYVARP WTVRQYAGFS TAEESNAFYR RNLAMGQKGL SVAFDLATHR GYDSDHPRVK
GDVGKAGVAI DSIEDMKILF DGIPLDKMSV SMTMNGAVLP ILAFYIVAAE EQGVKPEQLA
GTIQNDILKE YMVRNTYIYP PEMSMKIIAD IFEYTSKFMP KFNSISISGY HIQEAGATND
IELAYTLADG LEYVRTGLKA GIDIDSFAPR LSFFWAIGMN YYMEVAKMRA ARRIWAQMMS
TFNPKNPKSL ALRTHSQTSG WSLTEQDPFN NVTRTLIEAN AAAMGHTQSL HTNALDEAIA
LPTDFSARIA RNTQLFLQEE TGMTKVIDPW GGSYYVEKLT KELTEKAWAL IEEIEELGGM
AKAIETGLPK MKVEESAAKR QAKIDSKSET IVGVNKYLLE TEEPIDILDI DNSLVRQKQI
ERLDKLKEER NEEEVQKHLT RLTHAAQSGE ENLLAVAIDA ARARASLGEI SDAIESVSGR
HKAVIRSISG VYSSNFSDDE LIQEVKQMTE EFLENEGRRP RILVAKMGQD GHDRGAKVVA
TGYADLGFDV DISPLFMTPE EAARMAVEND VHCVGVSSLA AGHKTLVPEL IEELQKLGRE
DIIVIVGGVI PAQDYEFIYN AGAVAIFGPG TVIPVSAIKI IEEIYKRLGY EEVSS
//
