ID A0A370EHY3_9FLAO Unreviewed; 711 AA.
AC A0A370EHY3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DEU42_1097 {ECO:0000313|EMBL:RDI09711.1};
OS Flavobacterium sp. AG291.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2184000 {ECO:0000313|EMBL:RDI09711.1, ECO:0000313|Proteomes:UP000254305};
RN [1] {ECO:0000313|EMBL:RDI09711.1, ECO:0000313|Proteomes:UP000254305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG291 {ECO:0000313|EMBL:RDI09711.1,
RC ECO:0000313|Proteomes:UP000254305};
RA Venturi V.;
RT "Genome sequencing of rice bacterial endophytes.";
RL Submitted (JUL-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}.
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:RDI09711.1}.
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DR EMBL; QQAR01000009; RDI09711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370EHY3; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000254305; 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: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:UP000254305}.
FT DOMAIN 580..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 78668 MW; EE51AAC58381E795 CRC64;
MRKNIQHIQL KPEADNQSVN AEQNSFLTAE GIEVKENYFQ KDIENLEHLE FGAGFAPNLR
GPYATMYVRR PWTVRQYAGF STAEESNAFY RRNLAAGQKG LSVAFDLATH RGYDSDHERV
VGDVGKAGVA IDSVEDMKVL FDQIPLNEMS VSMTMNGAVL PIMAFYIVAA EEQGVAPELL
SGTIQNDILK EFMVRNTYIY PPAPSMKIIA DIFEYTSRKM PKFNSISISG YHMQEAGATA
DIELAYTLAD GLEYIRTGLA AGMKIDEFAP RLSFFWAIGM NHFMEIAKMR AGRMLWAKLL
KQFDPKDDKS LALRTHCQTS GWSLTEQDPF NNVARTAIEA AAAAFGGTQS LHTNALDEAI
ALPTDFSARI ARNTQIFLQE ETKITKTVDP WAGSYYVESL TDEIAKKAWA LIEEVEELGG
MTKAIEAGIP KLRIEEAAAR KQARIDSGQD IIVGVNKYRL EKEDPLHILD VDNQMVRRQQ
IERLDQIKAT RDTQKVKECL AKLTESAKSG EGNLLELAVD AARNRATLGE ISDALETIFG
RYKAQIKSFS GVYSKEIKND ESFEKAKQLA DAFAKLEGRR PRIMIAKMGQ DGHDRGAKVV
ATGYADVGFD VDIGPLFQTP AEAAKQAVEN DVHILGVSSL AAGHKTLVPQ VIEELKKYGR
EDIMVIVGGV IPAQDYQYLF DSGAVAVFGP GTKISDAAIK ILEVLIKGFE E
//
