ID A0A0T5NTK0_9RHOB Unreviewed; 710 AA.
AC A0A0T5NTK0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=XM53_11555 {ECO:0000313|EMBL:KRS12280.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS12280.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS12280.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS12280.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-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:KRS12280.1}.
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DR EMBL; LAXJ01000010; KRS12280.1; -; Genomic_DNA.
DR RefSeq; WP_057793460.1; NZ_LAXJ01000010.1.
DR AlphaFoldDB; A0A0T5NTK0; -.
DR STRING; 1641875.XM53_11555; -.
DR PATRIC; fig|1641875.4.peg.95; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000051295; 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:UniProtKB-EC.
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, ECO:0000313|EMBL:KRS12280.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 579..710
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 710 AA; 77615 MW; 3F8B30EB4217847B CRC64;
MGSKTDDWRK IAEGELKGRP LEDLTWKTLE GIDVKPLYTE EDVEGMDHLG TIPGQAPFTR
GVKATMYAGR PWTIRQYAGF STAEESNAFY RRNLAAGQQG VSVAFDLATH RGYDSDHPRV
VGDVGKAGVA IDSVEDMKIL FDGIPLDQVS VSMTMNGAVI PVLASFIVAG EEQGHDRSAL
SGTIQNDILK EFMVRNTYIY PPEPSMRIVS DIIEFTANEM PRFNSISISG YHMQEAGANL
VQELAYTLAD GREYVKAAIE AGMDVDRFAG RLSFFFAIGM NFFMEAAKLR AARLLWHRIM
TEFGAKNDRS KMLRTHCQTS GVSLQEQDPY NNVVRTAYEA MSAVLGGTQS LHTNALDEAI
ALPTDFSARI ARNTQLILQE ETGVTAVVDP LAGSYYVESL TAELAEKAWE LMEEVEEMGG
MTKAVASGMP KLRIEESAAT RQAMIDRGDE VIVGVNKYRK DKEDPIDILD VDNVKVRKGQ
VEALERIRAE RDEDACTKAL DELTRRAKDG GNLLEAAVEA ARARATVGEI SMAMEKEFGR
HRAEVKTLAG VYGKAYEGDE GFAAIQKSVE AFAEDEGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPD EAAQDAIDND VHVIGISSQA AGHKTLAPQL IDALKEKDAG
DIIVICGGVI PQQDYEFLKG VGVKAIFGPG TNIPEAAQDI LRLIREARVA
//
