ID A0A2K8V980_9FLAO Unreviewed; 687 AA.
AC A0A2K8V980;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=BTO06_03085 {ECO:0000313|EMBL:AUC14194.1};
OS Tenacibaculum sp. SZ-18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=754423 {ECO:0000313|EMBL:AUC14194.1, ECO:0000313|Proteomes:UP000232695};
RN [1] {ECO:0000313|EMBL:AUC14194.1, ECO:0000313|Proteomes:UP000232695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZ-18 {ECO:0000313|EMBL:AUC14194.1,
RC ECO:0000313|Proteomes:UP000232695};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) 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; CP019335; AUC14194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8V980; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000232695; 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:UP000232695}.
FT DOMAIN 556..687
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 687 AA; 75910 MW; F866F73CED6EA8C2 CRC64;
MSRKDISNIQ LEKNVSTTNQ RLKHEDFVAG LAPNLRGPYS TMYVRRPWTI RQYAGFSTAE
ESNAFYRRNL AAGQKGLSVA FDLATHRGYD SDHERVQGDV GKAGVAIDSV EDMKVLFDQI
PLDKMSVSMT MNGAVLPILA FYIIAAEEQG VTPEKLSGTI QNDILKEFMV RNTYIYPPTP
SMKIIADIFE YTSNNMPKFN SISISGYHMQ EAGATPEIEL AYTLADGLEY IKTGLAAGMD
IDTFAPRLSF FWAIGMDHFR EIAKMRAARM LWAKLVKQFN PKNPKSLALR THCQTSGWSL
TEQDPFNNVA RTTIEAMAAA FGGTQSLHTN ALDEAIALPT DFSARIARNT QIYLQQETNI
TKTVDPWAGS YHLEQLTEEI ANKAWELIQE TEELGGMTKA IEKGIPKMRI EEAAAIKQAK
IDSGQDIIVG VNKYQLEQED PLHILEVDNE AVRKSQIERL EYLKSKRDTF KVEACLKDLT
ECAKTGNGNL LDLAVKAARN RASLGEISDA LEAVFGRHKA VHKTISGVYS KEIKDDSLFK
KASELADEFA NLEGRRPRIM IAKLGQDGHD RGAKVVATGY ADLGFDVDVG PLFQTPKEAA
KQAIENDVHI IGISSLAAGH KTLVPQVIEE LKGYGREDIM VIVGGVIPAQ DYQFLFDSGA
VGVFGPGTKI AQAAIDMLEI LIDSIDE
//
