ID A0A087N241_9BACI Unreviewed; 716 AA.
AC A0A087N241;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=CH76_08165 {ECO:0000313|EMBL:KFL43194.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43194.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL43194.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43194.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) 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:KFL43194.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPUW01000020; KFL43194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087N241; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR Proteomes; UP000029097; 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:KFL43194.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029097}.
FT DOMAIN 580..712
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 716 AA; 78894 MW; 7739005824EEFA64 CRC64;
MKPNFDAVNI EEVLTTTQPA ASEETFLTNE GIDVKDVYMK EDLAGVKHLK DVSGVAPNTR
GPYPTMYVAR PWTVRQYAGF STAEESNAFY KRNLAMGQKG LSVAFDLATH RGYDSDHPRV
TGDVGKAGVA IDSIEDMKIL FDSIPLDQMS VSMTMNGAVL PILAFYIVAA EEQGVGPEKL
AGTIQNDILK EYMVRNTYIY PPAMSMQIIA DIFEYTSKFM PKFNSISISG YHIQEAGATN
DIELAYTLAD GLEYVRTGLK AGIDIDSFAP RLSFFWAIGM NYYMEVAKMR AARRIWAQMM
STFNPKNTKT LALRTHSQTS GWSLTEQDPF NNVARTLFEA NASSMGHTQS LHTNALDEAI
ALPTDFSARI ARNTQLFLQE ETGMTKVIDP WGGSYYVEKL TDEITKSAWA LIEEIEELGG
MAKAIDTGLP KMKVEEAAAK RQAKIDSKTE TIVGVNKYRL DVEEPIDILD IDNTLVRQKQ
IERLNTMKAN RDEAEVQKHL ARLTAAAKTG AENLLAVAVD AARARASLGE ISDAVEDVSG
RHKAVIRSIS GIYSSNFSDE EQLREIKQMT EEFEENEGRR PRILVAKMGQ DGHDRGAKVI
STAYADMGFD VDISPLFMTP AETAQMAVEN DVHVVGVSSL AAGHKTLVPE LYGELDKLGR
SDIVIVCGGV IPAQDYDFLY ANGASAIFGP GTVIPVSAQK TLEEVYRRLG YEEVSK
//
