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Database: UniProt
Entry: A0A1T5FVI2_9FLAO
LinkDB: A0A1T5FVI2_9FLAO
Original site: A0A1T5FVI2_9FLAO 
ID   A0A1T5FVI2_9FLAO        Unreviewed;       706 AA.
AC   A0A1T5FVI2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=SAMN05660477_02340 {ECO:0000313|EMBL:SKC00203.1};
OS   Soonwooa buanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Soonwooa.
OX   NCBI_TaxID=619805 {ECO:0000313|EMBL:SKC00203.1, ECO:0000313|Proteomes:UP000191112};
RN   [1] {ECO:0000313|EMBL:SKC00203.1, ECO:0000313|Proteomes:UP000191112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22323 {ECO:0000313|EMBL:SKC00203.1,
RC   ECO:0000313|Proteomes:UP000191112};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUYZ01000008; SKC00203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5FVI2; -.
DR   STRING; 619805.SAMN05660477_02340; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000191112; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191112}.
FT   DOMAIN          578..706
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   706 AA;  78097 MW;  0C8CFED8E942C2A7 CRC64;
     MRQAIKATKP DFNIQYTEPE IYYFEKDGLQ LKSSYTAADS QNLTEKSYSA GIAPYLRGPY
     STMYVQKPWT IRQYAGFSTA EESNAFYRRN LAAGQKGLSV AFDLATHRGY DSDHPRVVGD
     VGKAGVAIDS VEDMKILFNE IPLDQISVSM TMNGAVLPIL SFYIVAAEEQ GVSQDLLSGT
     IQNDILKEFM VRNTYIYPPT PSMKIIADIF EYTSKNIPKF NSISISGYHM QEAGATPVLE
     MAYTLADGLE YVRTGIKAGM NVDDFAPRLS FFWAIGMNHF MEIAKMRAAR YIWANLLTQF
     NPQNQKSLAL RTHSQTSGWS LTEQEPFNNI TRTAIEALSS ALGGTQSLHT NALDEAIALP
     TDYSAKIARN TQIILQQESG ICNVVDPMGG SDLVEALTQQ MIEEAMKYID EVEKEGGMTK
     AIEAGIPKMR IEEAAAIKQA KIDSGEEFII GVNSFKSQLK QEDIEILDID NSVVRQKQIE
     RLNNIKATRD NAAVEDILNQ IRQSAKTTEG NLLALCIEAA RRRVTLGEMS DAMEESFGRY
     KANIKTISGV YAMNAGKNEY FDKAVKLTEK FEEEEGRRPR IMVAKMGQDG HDRGAKVVAT
     AFADMGFDVD VAPLFQTPEE VAKQAIENDI HILGVSSLAA GHKTLVPQVV EELKKLGAED
     ITVVVGGVIP QQDYEFLYAN GADHIFGPGT NLPKCAVEIL EKMLVK
//
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