ID A0A0B5DXB8_9RHOB Unreviewed; 707 AA.
AC A0A0B5DXB8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=P73_3368 {ECO:0000313|EMBL:AJE48083.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE48083.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE48083.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE48083.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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}.
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DR EMBL; CP004393; AJE48083.1; -; Genomic_DNA.
DR RefSeq; WP_043870487.1; NZ_FNNW01000002.1.
DR AlphaFoldDB; A0A0B5DXB8; -.
DR STRING; 1208324.P73_3368; -.
DR KEGG; cid:P73_3368; -.
DR HOGENOM; CLU_009523_3_1_5; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000031521; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AJE48083.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031521}.
FT DOMAIN 579..707
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT COILED 485..512
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 707 AA; 76826 MW; 0BA85583DDB0A58E CRC64;
MTDRTKWEEL ATKELRGKPL ESLDWDTLEG IRVKPLYAED DLAGLSHLGN TPGVAPFTRG
VKATMYAGRP WTIRQYAGFS TAEESNAFYR KALAAGQQGV SVAFDLATHR GYDSDHPRVV
GDVGKAGVAI DSVEDMKILF DGIPLDQVSV SMTMNGAVIP VLASFIVVGE EQGHDRSVLS
GTIQNDILKE FMVRNTYIYP PEPSMRIIAD IIEYTSNEMP KFNSISISGY HMQEAGANLV
QELAFTLADG REYVRTAIRA GMDVDKFAGR LSFFFAIGMN FFMEAAKLRA ARLLWSRVME
EFAPKLDKSK MLRTHCQTSG VSLQEQDPYN NVIRTAYEAM SAALGGTQSL HTNALDEAIA
LPTEFSARIA RNTQLILQEE TGITHVVDPL AGSYYVESLT AELAGKAWAL MEEIEAMGGM
TKAVNSGMPK LRIEETAARR QAQIDRGEEV IVGVNKYRKD KEDPIDILDV DNVAVRNSQI
ARLDRIKASR DAARVEETLA ALEAAAKSGE GNLLALAVEA ARARATVGEI SMAMEKAFGR
HRAEVKTLAG VYGAAYEGDE GFAQIQRDVE AFAEREGRRP RMLVVKMGQD GHDRGAKVIA
TAFADIGFDV DVGPLFQTPE EAAQDAIDND VHIVGISSQA AGHKTLAPKL IEALKAQGAG
DIIVICGGVI PQQDYEFLYK AGVKAIFGPG TNIPAAARQI LDLIGTA
//
