ID A0A286GEC2_9ACTN Unreviewed; 735 AA.
AC A0A286GEC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=SAMN06272739_0454 {ECO:0000313|EMBL:SOD93842.1};
OS Blastococcus haudaquaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOD93842.1, ECO:0000313|Proteomes:UP000219482};
RN [1] {ECO:0000313|Proteomes:UP000219482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA Varghese N., Submissions S.;
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 -!- 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; OCNK01000001; SOD93842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GEC2; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000219482; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219482}.
FT DOMAIN 604..735
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 735 AA; 79452 MW; 63E10447E8CDD29A CRC64;
MSRIPDFGSV DLGRPSAGAT ADDWAKAFKE TTGRGVEEST WETPEGIAVP PLFTHEHLDG
LDFLGTYPGV APYLRGPYPT MYTTQPWTVR QYAGFSTATE SNAFYRRNLA AGQKGLSVAF
DLPTHRGYDS DHPRVPGDVG MAGVAIDSIL DMRQLFDGIP LDRMSVSMTM NGAVLPVLAL
YIVAAEEQGV SPDQLTGTIQ NDILKEFMVR NTYIYPPKPS MQIISDIFAF TSQRMPKFNS
ISISGYHIQE AGATADLELA YTLADGVEYL KAGQAAGMDV DAFAPRLSFF WAIGMNFFME
VAKLRAGRLL WAKLVKEAGA KNPKSLSLRT HSQTSGWSLT AQDVYNNVVR TCLEAMAATQ
GHTQSLHTNA LDEALALPTD FSARIARNTQ LLLQQESGTT RVIDPWGGSA YVEKLTYDLA
RRAWAHIQEV TEHGGMAQAI DDGIPKLRIE EAAARTQARI DSGRQPVIGV NKYRVEADEA
IEVLRVDNAD VLAQQKAKLE ELRASRDGEA VQEHLRRLTD AARAAADGKR GSELDSNLLK
LAVDAARAKA TVGEISDALE EVYGRHAGQV RTISGVYREE AGASGPMEET RRMAEAFADA
EGRRPRILVA KMGQDGHDRG QKVIATAFAD LGFDVDVGPL FQTPEEVARQ AVEADVHVVG
VSSLAAGHLT LVPALKKALA DLGADDVMIV VGGVIPPDDV PTLKEMGAAA VFLPGTVIAE
AAQDLLRALS ERLGH
//
