ID A0A3L8P749_9ACTN Unreviewed; 663 AA.
AC A0A3L8P749;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=D9V37_03750 {ECO:0000313|EMBL:RLV51045.1};
OS Nocardioides mangrovicus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2478913 {ECO:0000313|EMBL:RLV51045.1, ECO:0000313|Proteomes:UP000281708};
RN [1] {ECO:0000313|EMBL:RLV51045.1, ECO:0000313|Proteomes:UP000281708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4Q3S-7 {ECO:0000313|EMBL:RLV51045.1,
RC ECO:0000313|Proteomes:UP000281708};
RA Li F.;
RT "Marmoricola sp. 4Q3S-7 whole genome shotgun sequence.";
RL Submitted (OCT-2018) 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:RLV51045.1}.
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DR EMBL; RDBE01000001; RLV51045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8P749; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000281708; 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 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:UP000281708}.
FT DOMAIN 529..662
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 663 AA; 71828 MW; D24577D3D781463F CRC64;
MTERDKPWVM RTYAGHSSAA DSNRLYRGNL AKGQTGLSVA FDLPTQTGYD PDSPLAKGEV
GKVGVPVPHL GEMRRLFEDI PLTGMNTSMT INATAMWLLA LYQVVAEEQN PSAEPAEVAA
QLAGTTQNDI IKEYLSRGTY VFPPEHSLRL IADVISYTVH QIPKWNPVNI CSYHLQEVGA
TPVQELAYSL CTAIAVLDEV KDAGQVSEED FGRVVGRISF FVNAGVRFVE EMCKMRAFVR
LWDEITRERY GVEDPKMRRF RYGVQVNSLG LTEAQPENNV QRIVLEMLGV TLSKDARARA
VQLPAWNEAL GLPRPWDQQW SLRLQQVLAV ESDLLEYDDI FEGSVVVEAK VEQLCADARA
EIDRVQAMGG AVAAVEYMKQ ALVSSHSARR GRIESGEEKI VGVNCYETTE PSPLTADLDT
AIQTADPEAE RSAIASLEAW RSERDDDGVR VALENLAAAA KTDTNLMAAT LEAARAGATT
GEWAGTLREV FGEYRAPTGV SGSAVAEAGA ELSELREKVK STGEELGGRL RLLVGKPGLD
GHSNGAEQVA VRARDAGFEV VYQGIRLTPE QIVSAAVAED VHAIGLSILS GSHMELVPDV
LAKMKQAGID DVPVIVGGII PASDARRLEE LGVAAVFTPK DFSLTESTSG IVDAIRRANG
LAV
//
