ID A0A1A9GQH2_9ACTN Unreviewed; 675 AA.
AC A0A1A9GQH2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mutB_2 {ECO:0000313|EMBL:ANH40316.1};
GN ORFNames=I601_3918 {ECO:0000313|EMBL:ANH40316.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH40316.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH40316.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH40316.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-2016) 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; CP015079; ANH40316.1; -; Genomic_DNA.
DR RefSeq; WP_068113452.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GQH2; -.
DR STRING; 1300347.I601_3918; -.
DR KEGG; ndk:I601_3918; -.
DR PATRIC; fig|1300347.3.peg.3925; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000077868; 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, ECO:0000313|EMBL:ANH40316.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077868}.
FT DOMAIN 542..671
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 675 AA; 73169 MW; 271E9E1FECDF08B4 CRC64;
MTEMERPLVD RPEKDRPWVM RTYAGHSTAQ ASNELYRNNL SKGQTGLSVA FDLPTQTGYD
PDSVMSTGEV GKVGVPVPHL GEMRHLFDDI PLTSMNTSMT INATAMWMLA MYQVVAEEQN
PDLTAEEVAA QLAGTTQNDI IKEYLSRGTY VFPPEHSLRL ISDMIAYTVH QIPKWNPINI
CSYHLQEAGA TPTQELAYAL CTAIAVLDQV KASGQVAEDD FEKVVGRISF FVNAGVRFVE
ETCKMRAFVE LWDEITRERY GVQDPKMRRF RYGVQVNSLG LTEAQPENNV QRIVLEMLGV
TLSKNARARA VQLPAWNEAL GLPRPWDQQW SLRLQQVLAF ESDLLEYEDI FDGSTVIAAK
VAELVEGARA EIDRVQAMGG AIAAVESGYM KEELVSAHAA RRARIESGQE IIVGVNKYET
TEPSPLTADV DGAIMMADPR AEQSARDSVT EWKAQRDEQQ VVDALAALAE AAKGSENLMA
ATLVAARAGA TTGEWAGTLR EVFGEFRAPT GVSGAVGVAG AGAEITAVRE RVRATGEELG
GRLRLLVGKP GLDGHSNGAE QVAVRARDAG FEVVYQGIRL TPEQIVSAAV AEDVHCVGLS
ILSGSHMELV PAVLQGLRDA GAADVPVIVG GIIPDSDARR LKEQGVAAVY TPKDFGLTEI
MGGIVDVIRA AHDLD
//