ID A0A363RPC1_9BURK Unreviewed; 724 AA.
AC A0A363RPC1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DCO45_10245 {ECO:0000313|EMBL:PWB18934.1};
OS Comamonas sp. JNW.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2170731 {ECO:0000313|EMBL:PWB18934.1, ECO:0000313|Proteomes:UP000251772};
RN [1] {ECO:0000313|EMBL:PWB18934.1, ECO:0000313|Proteomes:UP000251772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JNW {ECO:0000313|EMBL:PWB18934.1,
RC ECO:0000313|Proteomes:UP000251772};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-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 -!- 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:PWB18934.1}.
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DR EMBL; QETI01000005; PWB18934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A363RPC1; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000251772; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000251772}.
FT DOMAIN 593..724
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 78006 MW; A78B6231133FD956 CRC64;
MTDSAKHNTA SEFPKADRAA WDKAASKSAP GGDVGSLDWL TPDGITVKPL YTAADTADLP
FADTLPGFAP YLRGPQATMY AVRPWTIRQY AGFSTAEESN AFYRKALAAG GQGVSVAFDL
ATHRGYDSDH PRVTGDVGKA GVAIDSVEDM KILFNSIPLD KVSVSMTMNG AVLPVLAGYV
VAAEEQGVAQ DQLSGTIQND ILKEFMVRNT YIYPPKPSMR IIGDIIEYTS QNMPKFNSIS
ISGYHMQEAG ANQALELAFT LADGKEYVKT AIAKGMDVDA FAGRLSFFWA VGMNFYLEIA
KMRAARLLWC RIMTGFEAKN PKSLMLRTHS QTSGWSLTEQ DPYNNVVRTT IEAMAAVFGG
TQSLHTNALD EAIALPTEFS ARIARNTQLI IQEETHITNV IDPWAGSYMM EKLTQDMADA
AWKIIEEVDA MGGMTQAVDS GWAKLKIEAA AAEKQARIDS GKEVIVGVNK YKLAKEDPVD
ILEVDNVKVR DSQIARLNQI KATRDAAAVG KALQALSAAA ESGEGNLLDL AIQAVRLRAT
VGEVSDALEK SFGRHRADTQ KVTGVYAAAY DSAEGWDKLK DEIAAFAEAQ GRRPRVMIAK
LGQDGHDRGA KVVATAFADL GYDVDMGPLF QTPEECARQA IENDVHAVGV STLAAGHKTL
VPAIIEELKK QGADDIIVFV GGVIPAQDYD YLYNAGVKGV YGPGTPIPAS AKDVLEQIKK
AVAV
//
