ID A0A1G9LI68_9ACTN Unreviewed; 735 AA.
AC A0A1G9LI68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN05660642_00437 {ECO:0000313|EMBL:SDL61604.1};
OS Geodermatophilus siccatus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137991 {ECO:0000313|EMBL:SDL61604.1, ECO:0000313|Proteomes:UP000198680};
RN [1] {ECO:0000313|EMBL:SDL61604.1, ECO:0000313|Proteomes:UP000198680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45419 {ECO:0000313|EMBL:SDL61604.1,
RC ECO:0000313|Proteomes:UP000198680};
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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; FNHE01000001; SDL61604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9LI68; -.
DR STRING; 1137991.SAMN05660642_00437; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000198680; 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.
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 604..735
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 735 AA; 79463 MW; 961AD5A61368F94C CRC64;
MSVIPDFGGV ELGRPAAAAS VDDWAKTFKE TTGRGVEEAA WETPEGIAVP PLFTPADLRG
LDFLATYPGI APYLRGPYPT MYTTQPWTVR QYAGFSTAAE SNAFYRRNLA AGQKGLSIAF
DLPTHRGYDS DHPRVVGDVG MAGVAVDSIL DMRQLFDGIP LDRMSVSMTM NGAVLPVLAL
YIVAAEEQGV EHGQLTGTIQ NDILKEFMVR NTYIYPPKPS MQIISDIFAF TSQEMPRFNS
ISISGYHIQE AGATADLELA YTLADGVEYL RAGKDAGLDV DAFAPRLSFF WAIGMNFFME
VAKLRAGRLL WARLVKEAGA QKDKSLSLRT HSQTSGWSLT AQDVYNNVVR TCLEAMAATQ
GHTQSLHTNA LDEALALPTD FSARIARNTQ LLLQQESGTT RVIDPWGGSA YVERLTYDLA
RRAWAHIEEV AEHGGMAQAI DDGIPKLRIE EAAARTQARI DSGRQPVIGV NKYRVDADEA
IEVLRVDNAD VLAQQKAKLE ELRASRDDGA VREALSRLTD AARAAAEGRR GRELDSNLLK
LAVDAARAKA TVGEISDALE EVYGRHAGQV RTISGVYRDE AGASGPMEET RRLAEAFEEA
EGRRPRILVA KMGQDGHDRG QKVIATAFAD LGFDVDVGPL FQTPEEVARQ AVEADVHVVG
VSSLAAGHLT LVPALKQALA DLGAEDVVIV VGGVIPPDDV PTLKEMGAAE VFLPGTVVAE
AAQRLLRTLS SNLGH
//
