ID A0A124I521_9ACTN Unreviewed; 682 AA.
AC A0A124I521;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AQJ64_02805 {ECO:0000313|EMBL:KUN88619.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN88619.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN88619.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN88619.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) 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}.
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:KUN88619.1}.
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DR EMBL; LMWW01000003; KUN88619.1; -; Genomic_DNA.
DR RefSeq; WP_055637318.1; NZ_LIQS01000484.1.
DR AlphaFoldDB; A0A124I521; -.
DR STRING; 1943.AQJ64_02805; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000052982; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 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:SF3; COENZYME B12-DEPENDENT MUTASE; 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.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 543..672
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 682 AA; 74735 MW; 80CA7E908D1A5E48 CRC64;
MTERQPAEGT REKDRPWLMR TYAGHSTAEA SNELYRRNLA KGQTGLSVAF DLPTQTGYDS
DHVLARGEVG RVGVPVAHLG DMRRLFQDIP LEQMNTSMTI NATAMWLLAL YQVVAEEQGA
DITRLQGTTQ NDIVKEYLSR GTHVFPPGPS LRLTTDMIAY TVSHIPKWNP INICSYHLQE
AGATPVQEIA YAMSTAIAVL DAVRDSGQVP AEKFGDVVAR ISFFVNAGVR FVEEMCKMRA
FGRIWDQVTR ERYGIENPKQ RRFRYGVQVN SLGLTEAQPE NNVQRIVLEM LAVTLSKDAR
ARAVQLPAWN EALGLPRPWD QQWSLRIQQV LAHESDLLEY EDLFEGSHVV EAKVARLVEE
SLAEIGRIQE MGGAMAAVES GYLKSQLVSS HAERRARIES GQEKIVGVNI FETTEPNPLT
ADLDTAIQTV DPAVEARVVA SLQHWRDTRY QPPFNHPRPC KALERLKEAA KGTDNLMEAT
LECARAGVTT GEWAGALREV FGEFRAPTGV SSAPVAVPAE EGSAMSEVRR RVETTAKDLG
TGKLRFLVGK PGLDGHSNGA EQIAVRARDA GFEVVYQGIR LTPEQIVDAA LAEDVHAVGL
SILSGSHAQL VPDVLQRLRV AGATDIPVIA GGIIPNGDAE QLRAAGVAAV FTPKDFDITG
IIGRIVDEIR KANKLDPLEV PA
//