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Database: UniProt
Entry: E9AD07_LEIMA
LinkDB: E9AD07_LEIMA
Original site: E9AD07_LEIMA 
ID   E9AD07_LEIMA            Unreviewed;       723 AA.
AC   E9AD07;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=LMJF_27_0300 {ECO:0000313|EMBL:CBZ12090.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ12090.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CBZ12090.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CBZ12090.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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; FR796423; CBZ12090.1; -; Genomic_DNA.
DR   RefSeq; XP_003721836.1; XM_003721788.1.
DR   AlphaFoldDB; E9AD07; -.
DR   STRING; 5664.E9AD07; -.
DR   EnsemblProtists; CBZ12090; CBZ12090; LMJF_27_0300.
DR   GeneID; 12982958; -.
DR   KEGG; lma:LMJF_27_0300; -.
DR   VEuPathDB; TriTrypDB:LmjF.27.0300; -.
DR   VEuPathDB; TriTrypDB:LMJFC_270008300; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_270008000; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_270007900; -.
DR   eggNOG; ENOG502QQ7X; Eukaryota.
DR   HOGENOM; CLU_009523_3_1_1; -.
DR   InParanoid; E9AD07; -.
DR   OMA; IQEETHI; -.
DR   Proteomes; UP000000542; Chromosome 27.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IBA:GO_Central.
DR   GO; GO:0019678; P:propionate metabolic process, methylmalonyl pathway; IBA:GO_Central.
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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CBZ12090.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT   DOMAIN          593..723
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   723 AA;  79306 MW;  8FEBF1CEA3B21D64 CRC64;
     MMRRVPVLLS AAYLPEWIAA AKKELKNRDP STLTIHSING FDIKPLYLAD DVESHPALPG
     FFPYTRGVHA TMYTGRPWTI RQYAGFSTAE ESNNFYKTAL KNGQQGLSVA FDLATHRGYD
     SDHPRVTGDV GMAGVAVDSV EDMKLLFNDI PLDKVSVSMT MNGAVIPVLA FFAVAAEESG
     VSQEKLRGTI QNDILKEFMV RNTYIFPPTP SMRILGDVMA YVSKRQPKFN SISISGYHIQ
     EAGGHGALEL AFTIADGLEY IRCAEQRGLT VDDVAPRFSF FFGIGMNFYC EIAKLRAART
     LWATYVKKKF NPKNPKSLLL RTHSQTSGWS LTEQDMENNI IRTTIEAMAA VMGGVQSLHT
     NAFDEAVALP SVQSSRIARN TQIIIQEETC ICSVVDPWGG SYMMEALTQE MIKKASAIID
     DVEAKGGMTK CIEEGFPKLM IEESAARRQA AIDSGAETIV GVNKYVNPVD KIHETLRIDD
     QKVRAGQIAA LEKLKATRDK AKVQEMLKKV TEACKDENVN ILEAAVEAAR ARATLGEITS
     AMEEVYGRYV AKNQVVQGVY YNSYLRGGNK EDQNHVAAVK ARVDAFAAKE GRRPRIMVAK
     IGQDGHDRGA KVVATGLADM GYDVDIGPLF QTPEEVARHA VENDVHICGA SSLAAGHRTL
     IPQLIQELKK LGADDIIVTA GGVIPPDDYQ SLYDAGVKLI FGPGTPIPKC AEQMIEVLEA
     RQK
//
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