ID A0A2A3JPA9_9RHOB Unreviewed; 711 AA.
AC A0A2A3JPA9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CLG85_22495 {ECO:0000313|EMBL:PBD17003.1};
OS Alloyangia mangrovi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Alloyangia.
OX NCBI_TaxID=1779329 {ECO:0000313|EMBL:PBD17003.1};
RN [1] {ECO:0000313|EMBL:PBD17003.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS 153D {ECO:0000313|EMBL:PBD17003.1};
RA Verma A., Krishnamurthi S.;
RT "Yangia sp. SAOS 153D whole genome sequencing.";
RL Submitted (SEP-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}.
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:PBD17003.1}.
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DR EMBL; NTHN01000478; PBD17003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3JPA9; -.
DR OrthoDB; 9762378at2; -.
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}.
FT DOMAIN 579..711
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 77629 MW; DD1E10D1E1316F41 CRC64;
MTAKKDEWRQ LAAKELRGRT LNDLTWHTLE GIEVQPLYTA EDTADLPHMG TLPGFGPFTR
GVKATMYAGR PWTIRQYAGF STAEDSNAFY RKALAAGQQG VSVAFDLATH RGYDSDHPRV
VGDVGKAGVA IDSVEDMKIL FDGIPLDKIS VSMTMNGAVI PILASFIVVG EEQGHDRAVL
SGTIQNDILK EFMVRNTYIY PPEPSMRIIS DIIEYTSNEM PKFNSISISG YHMQEAGANL
VQELAYTLAD GREYVRAAIN AGMDVDKFAG RLSFFFAIGM NFFMEAAKLR AARTLWHRIM
TEFGAKSDRS KMLRTHCQTS GVSLQEQDPY NNVIRTAYEA MSAVLGGTQS LHTNALDEAI
ALPTEFSARI ARNTQLILQE ETGVTNVVDP LAGSYYVESL TAELIDKAWA LIEEVEEMGG
MTKAVASGMP KLRIEETAAR RQAQIDRGEE VIVGVNKYRK DREDPIDILD IDNAKVRDSQ
VARLEHVRAT RDQAKCDAAL AELERRAKEG GNLLEAAVEA ARARASVGEI SMAMEKEFGR
HRAEVKTLAG VYGAAYEGDE GFAQIQRDVE SFAEAEGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPE EAAQDAIDND VHIVGISSQA AGHKTLAPQL VQALKEQGAE
DIIVICGGVI PQQDYDFLYK AGVKAIFGPG TNIPSAAKQI LGLIGAPRAA E
//
