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Database: UniProt
Entry: E1Z2B7_CHLVA
LinkDB: E1Z2B7_CHLVA
Original site: E1Z2B7_CHLVA 
ID   E1Z2B7_CHLVA            Unreviewed;       780 AA.
AC   E1Z2B7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   ORFNames=CHLNCDRAFT_18280 {ECO:0000313|EMBL:EFN59631.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN59631.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN59631.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
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; GL433835; EFN59631.1; -; Genomic_DNA.
DR   RefSeq; XP_005851733.1; XM_005851671.1.
DR   AlphaFoldDB; E1Z2B7; -.
DR   STRING; 554065.E1Z2B7; -.
DR   GeneID; 17359503; -.
DR   KEGG; cvr:CHLNCDRAFT_18280; -.
DR   eggNOG; ENOG502QQ7X; Eukaryota.
DR   InParanoid; E1Z2B7; -.
DR   OMA; IQEETHI; -.
DR   OrthoDB; 304517at2759; -.
DR   Proteomes; UP000008141; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 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:ARBA00022628};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141}.
FT   DOMAIN          640..773
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   780 AA;  84199 MW;  764E99FA6A9E328F CRC64;
     MGIPRALARL GPQGLRAVRG YASAAGGATE QNLEEWKQRA GKEAKGRDPW QAFSSTNQDI
     HLMPVYSGLD VAGQPDYGSE FPGVYPYTRG PYASMYTGRP WTIRQYAGFS TAEESNAFYR
     KALAAGQQGT SIAFDLPTHR GYDSDHPRVS GDVGMAGVAV DSVEDMKILF DQIPLDRMSV
     SMTMNGAVLP VMAMFVVAAE EQGVAAAKLQ GTIQNDILKA RRRERPWQGR GKAEGEFMVR
     NTYIYPPHPS MRIVGDIFAY CSRHLPKFHP ISISGYHMQE AGATPGLELA FTLADGLEYI
     RCAEQAGLTV DQVAPRLSFF FAIGMDFFSE VAKLRAARRL WARLVKEKFG PSDEKSLVLR
     THCQTSGYSL TAQEPYNNII RTTVEAMAAV MGGTQSLHTN SFDEAIALPT DFSAKLARNT
     QLILAEETGI TKACVADPLG GSFYLEALTS QMEAAAEEVI REVEQMGGMT EAIISGLPKL
     KIEECAARQQ AHIDSNKQAP LQVIVGVNKY AQGDDNGGAP RELDVRRIDN TMVLQRQQER
     LAQSLRATRD EAAVQAALAA LEAAAHSGNR QHNLMELAVQ AARLRATVGD ISAALEKAWG
     RYEAGGGMST GVYNKALGTS AQMEAVQRVV ARFEAEVGRH PRILIAKMGQ DGHDRGAKVM
     ATGLADLGFD VDIGPLFMTP HEVARHAVDA DVHVVGVSSQ AAGHGTLVPE LMRELAAQGM
     GHVLVVCGGI IPKQASGLRR WRAWVAAFYG PGTRVPAAAL DMIGMLLEGK QPEAGSQGTA
//
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