ID R7XZ02_9ACTN Unreviewed; 681 AA.
AC R7XZ02;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=CF8_1438 {ECO:0000313|EMBL:EON24523.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON24523.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON24523.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON24523.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(2013).
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:EON24523.1}.
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DR EMBL; ASEP01000047; EON24523.1; -; Genomic_DNA.
DR AlphaFoldDB; R7XZ02; -.
DR STRING; 110319.CF8_1438; -.
DR PATRIC; fig|110319.3.peg.2029; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_4_0_11; -.
DR Proteomes; UP000015971; 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 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:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015971}.
FT DOMAIN 548..677
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 73514 MW; 1B40DF9FD3879D8C CRC64;
MLMTDKQVDA TPAEAARPEK DRPWVMRTYA GHSTAAASNA LYRGNLAKGQ TGLSVAFDLP
TQTGYDPDSP LSRGEVGKVG VPIPHLGEMR RLFEDIPLTG MNTSMTINAT AMWMLAMYQV
AAEEQNPGVD VREVAAQLAG TTQNDIIKEY LSRGTYVFPP EHSLRLISDM IAYTVHEIPK
WNPINICSYH LQEAGATPTQ ELAYALCTAI AVLDQVRNSG QVSEDDFEKV VGRISFFVNA
GVRFVEETCK MRAFVQLWDE ITRERYGVQD EKMRRFRYGV QVNSLGLTEA QPENNVQRIV
LEMLGVTLSK NARARAVQLP AWNEALGLPR PWDQQWSLRL QQVLAFESDL LEYDDIFDGS
HVIAAKVASL VEGAKAEIDR VQAMGGAIAA VESGYMKQAL VSAHAARRAR IEAGEEIIVG
VNKFDTTEAS PLTANLDDAI MAADPKAEQT ARDSVTAWKE QRDEAAVTAA LEALAAEAKT
DKNLMHATLA AARAGATTGE WAGTLREVFG EFRAPTGVSG AVGVVEAGAE LTAVREKVRA
TGEELGGRLR LLVGKPGLDG HSNGAEQVAV RARDAGFEVI YQGIRLTPEQ IVAAAIAEDV
HCVGLSILSG SHMELVPDVL AGLREAGLDD IPVIVGGIIP ESDGKRLMEQ GVAAVYTPKD
FGLTAIMGGI VDVIRKANDL A
//
