ID A0A2S1QXW1_9FLAO Unreviewed; 713 AA.
AC A0A2S1QXW1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=HYN59_09020 {ECO:0000313|EMBL:AWH85250.1};
OS Flavobacterium album.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2175091 {ECO:0000313|EMBL:AWH85250.1, ECO:0000313|Proteomes:UP000244929};
RN [1] {ECO:0000313|EMBL:AWH85250.1, ECO:0000313|Proteomes:UP000244929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0059 {ECO:0000313|EMBL:AWH85250.1,
RC ECO:0000313|Proteomes:UP000244929};
RA Yi H., Baek C.;
RT "Genome sequencing of Flavobacterium sp. HYN0059.";
RL Submitted (APR-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}.
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DR EMBL; CP029186; AWH85250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1QXW1; -.
DR KEGG; falb:HYN59_09020; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000244929; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000244929}.
FT DOMAIN 581..713
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 78897 MW; 3DB034D997800862 CRC64;
MSRKNLQHIK LHGSPKPETR NTEQDNFVIA EGIAVKQNYT AEDIENLEHI AFGAGFAPNL
RGPYATMYVR RPWTIRQYAG FSTAEESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDHER
VVGDVGKAGV AIDSVEDMKV LFDQIPLDEM SVSMTMNGAV LPIMAFYIVA AEEQGVKPEL
LSGTIQNDIL KEFMVRNTYI YPPTPSMRII ADIFEYTSRK MPKFNSISIS GYHMQEAGAT
ADIELAYTLA DGLEYIRTGL AAGMKIDDFA PRLSFFWAIG MNHFMEIAKM RAGRMLWAKL
LKQFEPKDEK SLALRTHCQT SGWSLTEQDP FNNVARTCIE AAAAAFGGTQ SLHTNALDEA
IALPTDFSAR IARNTQIFLQ EETKITKTVD PWAGSYYIES LTDEIAKKAW ALIEEVEELG
GMTKAIEAGI PKLRIEEAAA RKQARIDSGQ DIIVGVNKYR LEKEDPLHIL DVDNQMVRRQ
QLEQLAKIKA SRDTKKVNEC LANLTAAAKS GEGNLLELAV EAARHRATLG EISDALETVY
GRYKAQIRSF SGVYSKEIKN DESFEKAKQL ADEFAKLEGR RPRIMIAKMG QDGHDRGAKV
VATGYADVGF DVDIGPLFQT PTEAAKQAVE NDVHILGVSS LAAGHKTLVP QVIEELKKYG
REDIMVIVGG VIPAQDYQYL FDSGAVAVFG PGTKISEAAI KILEVLIKGF EEL
//