ID A0A1G8Z407_9RHOB Unreviewed; 714 AA.
AC A0A1G8Z407;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN04488026_10316 {ECO:0000313|EMBL:SDK09859.1};
OS Aliiruegeria lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=571298 {ECO:0000313|EMBL:SDK09859.1, ECO:0000313|Proteomes:UP000199382};
RN [1] {ECO:0000313|EMBL:SDK09859.1, ECO:0000313|Proteomes:UP000199382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25294 {ECO:0000313|EMBL:SDK09859.1,
RC ECO:0000313|Proteomes:UP000199382};
RA de Groot N.N.;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNEK01000031; SDK09859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8Z407; -.
DR STRING; 571298.SAMN04488026_10316; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000199382; 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:UP000199382}.
FT DOMAIN 581..713
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 714 AA; 78243 MW; C71A8F30725FCB5A CRC64;
MTDIKTPQDW AELATKELRG KPLDALTWET LEGIKVKPLY TEEDIKGLPH MGSLPGFEPF
TRGPKATMYA GRPWTIRQYA GFSTAEESNA FYRRALAAGQ QGVSVAFDLA THRGYDSDHP
RVEGDVGKAG VAIDSVEDMK ILFDGIPLDK VSVSMTMNGA VIPVLANFIV VGEEQGHDKS
VLAGTIQNDI LKEFMVRNTY IYPPEPSMRI IGDIIEYTAN EMPKFNSISI SGYHMQEAGA
DLVQELAFTL ADGREYVRTA IKAGMPVDKF AGRLSFFFCM GMNFFMEIAK LRAARTLWSR
VMTDLGAKDP RSKMLRTHCQ TSGVSLAEQD PYNNVIRTAY EAMSAALGGT QSLHTNALDE
AIALPTDFSA RIARNTQIIL QEETQVTKVV DPLAGSYYVE ALTNELIEKA WALMEEVEEL
GGMTAAVNSG MPKLRIEESA AKRQSMIDRG EEVIVGVNKH KLAKEDELEI LDVDNVAVRK
SQIERLEKMR STRDEAACQA ALEEITRRTT EGGNLLEAAV DAARARASVG EISMAMEKVF
GRHRAEIKTL SGVYGAAYEG DDEFIAIQKS IEEFAEKEGR RPRMLVVKMG QDGHDRGAKV
IATAYADIGF DVDVGPLFQT PEEAAQDAID NDVHIVGISS LAAGHKTLAP RLVEELKKQG
AEDIIVICGG VIPHQDYEFL YNAGVSAIFG PGTNIPASAQ EIMNIISKKR ETAA
//
