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Database: UniProt
Entry: I0HNJ2_RUBGI
LinkDB: I0HNJ2_RUBGI
Original site: I0HNJ2_RUBGI 
ID   I0HNJ2_RUBGI            Unreviewed;       723 AA.
AC   I0HNJ2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   OrderedLocusNames=RGE_12380 {ECO:0000313|EMBL:BAL94579.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL94579.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL94579.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL94579.1; -; Genomic_DNA.
DR   RefSeq; WP_014427450.1; NC_017075.1.
DR   AlphaFoldDB; I0HNJ2; -.
DR   STRING; 983917.RGE_12380; -.
DR   KEGG; rge:RGE_12380; -.
DR   PATRIC; fig|983917.3.peg.1205; -.
DR   eggNOG; COG1884; Bacteria.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_3_1_4; -.
DR   Proteomes; UP000007883; 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.
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:BAL94579.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883}.
FT   DOMAIN          593..723
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   723 AA;  78315 MW;  35A0EA165B069549 CRC64;
     MSNSPDPLKS GEFAPSSLEQ WQKAAAKSAP GGDVEALNWQ TPEGLTVKPL YTAADTAELP
     YADTLPGFEP FIRGPQATMY AVRPWTIRQY AGFSTAEESN AFYRKALAAG GQGVSVAFDL
     ATHRGYDSDH PRVTGDVGKA GVAIDSVEDM KILFDAIPLD KVSVSMTMNG AVLPVLAGYV
     VAAEEQGVAQ ELLSGTIQND ILKEFMVRNT YIYPPEPSMR IVADIIEYTA RHMPKFNSIS
     ISGYHMQEAG ANQALELAFT LADGKEYVKT AIARGLDVDE FAGRLSFFWA IGMNFYLEIA
     KMRAARLLWC RIMKGFNAKK PKSLMLRTHC QTSGWSLTEQ DPYNNIVRTT VEAMAAVFGG
     TQSLHTNSFD EAIALPTEFS SRIARNTQLI IQEETHITKV VDPWAGSYLM EKLTQDMADK
     AWAIIEEVEA MGGMTRAVDS GWAKLKIEAS AAEKQARIDS GQDVIVGVNK YRNSKQDKVE
     ILEVDNVKVR DAQIARLAQV RAARDGAKVQ AALEALTAAA HSGEGNLLGL AIDAMRVRAT
     VGEVSDALEK IFGRHRADIQ KVTGVYAAAY DSAEGWDKLK AEIDEFAEQQ GRRPRVMIAK
     LGQDGHDRGA KVVATAFADL GFDVDIGALF QTPEECARQA IENDVHAVGV STLAAGHKTL
     VPAIIKALKD QGADDIVVFA GGVIPQQDYD FLFEAGVKGI YGPGTPVPAS AKDVLEQIKK
     AVG
//
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