ID A0A0P7AYW9_9FLAO Unreviewed; 689 AA.
AC A0A0P7AYW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=I595_2168 {ECO:0000313|EMBL:KPM31673.1};
OS Croceitalea dokdonensis DOKDO 023.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceitalea.
OX NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM31673.1, ECO:0000313|Proteomes:UP000050280};
RN [1] {ECO:0000313|EMBL:KPM31673.1, ECO:0000313|Proteomes:UP000050280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM31673.1,
RC ECO:0000313|Proteomes:UP000050280};
RA Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT 023 that contains proton- and sodium-pumping rhodopsins.";
RL Submitted (SEP-2015) 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:KPM31673.1}.
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DR EMBL; LDJX01000004; KPM31673.1; -; Genomic_DNA.
DR RefSeq; WP_054559259.1; NZ_LDJX01000004.1.
DR AlphaFoldDB; A0A0P7AYW9; -.
DR STRING; 1300341.I595_2168; -.
DR PATRIC; fig|1300341.3.peg.2342; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000050280; 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.
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:UP000050280}.
FT DOMAIN 561..689
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 689 AA; 75848 MW; B0B689B9458DC7BB CRC64;
MSRKNLQDIQ LKDFGPASTK QHTGFDFAAG MPPFLRGPYS TMYVRRPWTI RQYAGFSTAE
ESNAFYRRNL EAGQKGLSVA FDLPTHRGYD SDNERVVGDV GKAGVAIDSV EDMKILFDQI
PLDKMSVSMT MNGAVLPIMA FYIVAAEEQG VGLDQLSGTI QNDILKEFMV RNTYIYPPTP
SMQIIADIFE YTSKQMPRFN SISISGYHMH EAGAPAALEV AYTLADGIEY IRTGLKAGLK
IDEFAPRLSF FWGIGMNHFT EIAKMRAARV LWTKLVRGFA PQNQKSLMLR THSQTSGWSL
TEQDPFNNVA RTTIEAMAAA FGGTQSLHTN ALDEAIALPT DFSARIARNT QIYLQKETEI
TRTVDPWAGS HYVEGLTMQI AQEAWKLIEE VEELGGMTKA IEAGIPKLRI EEAAAKKQAR
LDSGQEVLVG VNKYVLEDED QLQILEVDNQ KVREQQVAGI AAIKNNRDAA KVSEALANIS
KAAHQKTKGE QGDNLLALAV VAARERATLG EISDAMETAF GRYRAKIQSI SGVYSKEIKK
DELFDKAKTM ANEFAASEGR RPRIMVAKMG QDGHDRGAKV VSTGYADLGF DVDIGPLFQT
PEEVAKQAVE NDVHILGISS LAGGHKTLVP AVVTELKKYG REDIIIIVGG VIPKQDYDFL
YEHGALAIFG PGTKISEAAI TILEILMDE
//
