ID C5T611_ACIDE Unreviewed; 722 AA.
AC C5T611;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, 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=AcdelDRAFT_2341 {ECO:0000313|EMBL:EER60078.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER60078.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER60078.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER60078.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
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:EER60078.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACQT01000076; EER60078.1; -; Genomic_DNA.
DR RefSeq; WP_005796755.1; NZ_ACQT01000076.1.
DR AlphaFoldDB; C5T611; -.
DR PATRIC; fig|573060.9.peg.2749; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000003856; 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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 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:EER60078.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856}.
FT DOMAIN 592..722
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 722 AA; 78060 MW; 401AFCFD1C8F5CA5 CRC64;
MSDTPKNNAP EFAASSLEAW AKAAAKSAPG GDVSALNWVT PDGITVKPLY TAEDTASLPY
ANTLPGFEPY LRGPQATMYA VRPWTIRQYA GFSTAEESNA FYRKALAAGG QGVSVAFDLA
THRGYDSDHP RVTGDVGKAG VAIDSVEDMK ILFDQIPLDK VSVSMTMNGA VLPVLAGYVV
AAEEQGVSQD KLSGTIQNDI LKEFMVRNTY IYPPKPSMRI IGDIIGYTAK NMPKFNSISI
SGYHMQEAGA NQALELAFTL ADGKEYVKTA IASGLDVDEF AGRLSFFWAI GMNFYLEVAK
MRAARLLWCR IMKETGAKNP KSLMLRTHCQ TSGWSLTEQD PYNNVVRTTI EAMAAVFGGT
QSLHTNALDE AIALPTEFSA RIARNTQLII QEETHITNVI DPWAGSYMME KLTQDMMDAA
WKIIEEVEAM GGMTQAVDSG WAKLKIEAAA AEKQARIDSG RDVIVGVNKY KLAKEDPVDI
LQIDNVKVRD GQIARLQKIR ATRDAAKVQA ALDALTAAAE SGQGNLLDLS IQAVRLRATV
GEVSDALEKV FGRHRADTQK VTGVYAAAYD SAEGWEKLKT EINAFAEEQG RRPRVMIAKL
GQDGHDRGAK VVATAFADLG FDVDMGPLFQ TPEECARQAI ENDVHAVGVS TLAAGHKTLV
PAIIQSLKEQ GADDIIVFVG GVIPAQDYEH LYQAGVKGIY GPGTPIPASA KDVLEQIRKA
LA
//
