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
//