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
//