ID H6RL31_BLASD Unreviewed; 735 AA.
AC H6RL31;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mutB2 {ECO:0000313|EMBL:CCG04998.1};
GN OrderedLocusNames=BLASA_4172 {ECO:0000313|EMBL:CCG04998.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG04998.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG04998.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG04998.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) 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; FO117623; CCG04998.1; -; Genomic_DNA.
DR RefSeq; WP_014377870.1; NC_016943.1.
DR AlphaFoldDB; H6RL31; -.
DR STRING; 1146883.BLASA_4172; -.
DR KEGG; bsd:BLASA_4172; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_11; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000007517; Chromosome.
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, ECO:0000313|EMBL:CCG04998.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT DOMAIN 604..735
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 735 AA; 79003 MW; 89C2F8CA70A3A73B CRC64;
MSTIPDFGSV ELGTPSGGTS ADDWAKAFEV TTGRGVAEAT WETPEGIAVP PLYTHEHLEG
LDFLETLPGL PPFLRGPYPT MYTTQPWTVR QYAGFSTATE SNAFYRRNLA AGQKGLSIAF
DLPTHRGYDS DHPRVPGDVG MAGVAIDSIL DMRQLFDGIP LDKMSVSMTM NGAVLPVLAL
YIVAAEEQGV EPGQLTGTIQ NDILKEFMVR NTYIYPPKPS MQIISDIFSF TSQKMPKFNS
ISISGYHIQE AGATADLELA YTLADGVEYL KAGQAAGMDV DAFAPRLSFF WAIGMNFFME
VAKLRAGRLL WAKLVKEAGA QNPKSLSLRT HSQTSGWSLT AQDVYNNVVR TCLEAMAATQ
GHTQSLHTNA LDEALALPTD FSARIARNTQ LLLQQESGTT RVVDPWGGSA YVEKLTYDLA
RRAWAHIEEV AEHGGMAQAI DDGIPKLRIE EAAARTQARI DSGRQPVIGV NKYRVDADEA
IEVHKVDNAD VLAQQKAKLE QLRGDRDGHA VTEALGRLTD AARAAADGRR GTDLDANLLK
LAVDAARAKA TVGEISDALE AVYGRHAGQV RTISGVYRDE AGASGPVDDT RRMAEEFAEA
EGRRPRILVA KMGQDGHDRG QKVIATAFAD LGFDVDVGPL FQTPDEVARQ AVEADVHVVG
VSSLAAGHLT LVPALKQALA DLGADDVLIV VGGVIPPDDV PTLKEMGAAA VFPPGTVIAE
AAQELLRTLS QRLGH
//
