ID A0A0Q7BBK2_9ACTN Unreviewed; 724 AA.
AC A0A0Q7BBK2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=ASC77_20915 {ECO:0000313|EMBL:KQW45258.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW45258.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW45258.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW45258.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW45258.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW45258.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW45258.1}.
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DR EMBL; LMDV01000012; KQW45258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7BBK2; -.
DR STRING; 1736439.ASC77_20915; -.
DR Proteomes; UP000051939; 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.
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:KQW45258.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 593..724
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 78896 MW; 7DC3931DAC78E0A9 CRC64;
MRDGRRRARL PDPNEGEARM TVPDSFSGEP WMSPEGIEIK PFYTESDLEG LDALGTFPGL
TPFLRGPYPT MYTTQPWTIR QYAGFSTAEE SNAFYRRNLA AGQKGLSVAF DLATHRGYDS
DHPRVRGDVG MAGVAIDSIY DTRTLFDGIP LDEMSVSMTM NGAVLPVLAL YIAAAEEQGV
KPEQLAGTIQ NDILKEFMVR NTYIYPPAPS MRIISDIFSY TSAKMPRFNS ISISGYHIQE
AGATADLELA YTLADGVEYI RAGLDTGMTI DQFAPRLSFF WAIGMNFFME IAKMRAARAL
WARLVREFDP QNPKSLSLRT HSQTSGWSLT AQDVFNNVGR TAIEAMAATQ GHTQSLHTNA
LDEAIALPTD FSARIARNTQ LLLQQESGTT GTIDPWAGSY YVERLTHDLA ERAWAHIQEA
EQAGGMAAAI EQGIPKMRIE EAAARTQARI DSGAQKVIGV NTYRLAAEDK LDVLKVDNDD
VYRQQVAKLE RLRAERDDDA VRRALEALTN SADRGATQGS LDGNLLALAV DAARAKATVG
EISDALEKVY GRHQAVIRTI SGVYRDESSQ GDGTLVQQVL DATEEFEEAE GRRPRILVAK
MGQDGHDRGQ KVIVSAFADM GFDVDVGPLF STPEEVAQQA VDADVHIVGV SSLAAGHLTL
LPALKSALAE QGRPDIMVVI GGVIPPDDVP TLQEMGAAAV FLPGTVIAES ALDLLAKLRE
QLDH
//
