MMAC_CAEEL
ID MMAC_CAEEL Reviewed; 272 AA.
AC Q7Z144;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=MMACHC-like protein;
DE EC=1.16.1.- {ECO:0000250|UniProtKB:Q9Y4U1};
DE AltName: Full=Cobalamin deficiency protein 1;
DE AltName: Full=Cyanocobalamin reductase (cyanide-eliminating);
GN Name=cblc-1; ORFNames=ZK546.17;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
RX PubMed=16843692; DOI=10.1016/j.ymgme.2006.06.001;
RA Chandler R.J., Aswani V., Tsai M.S., Falk M., Wehrli N., Stabler S.,
RA Allen R., Sedensky M., Kazazian H.H., Venditti C.P.;
RT "Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans:
RT evidence for a role of methylmalonyl-CoA epimerase in intermediary
RT metabolism.";
RL Mol. Genet. Metab. 89:64-73(2006).
CC -!- FUNCTION: Catalyzes the reductive dealkylation of cyanocobalamin to
CC cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate.
CC Can also catalyze the glutathione-dependent reductive demethylation of
CC methylcobalamin, and, with much lower efficiency, the glutathione-
CC dependent reductive demethylation of adenosylcobalamin. Under anaerobic
CC conditions cob(I)alamin is the first product; it is highly reactive and
CC is converted to aquocob(II)alamin in the presence of oxygen. Binds
CC cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related
CC vitamin B12 derivatives. {ECO:0000250|UniProtKB:Q9Y4U1}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4U1};
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4U1};
CC Note=Can utilize both FAD and FMN. {ECO:0000250|UniProtKB:Q9Y4U1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4U1}.
CC -!- SIMILARITY: Belongs to the MMACHC family. {ECO:0000305}.
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DR EMBL; FO081669; CCD73227.1; -; Genomic_DNA.
DR RefSeq; NP_001022524.1; NM_001027353.4.
DR PDB; 5UJC; X-ray; 1.35 A; A=1-264.
DR PDBsum; 5UJC; -.
DR AlphaFoldDB; Q7Z144; -.
DR SMR; Q7Z144; -.
DR STRING; 6239.ZK546.17; -.
DR PaxDb; Q7Z144; -.
DR PeptideAtlas; Q7Z144; -.
DR EnsemblMetazoa; ZK546.17.1; ZK546.17.1; WBGene00022766.
DR GeneID; 3565644; -.
DR KEGG; cel:CELE_ZK546.17; -.
DR CTD; 3565644; -.
DR WormBase; ZK546.17; CE34461; WBGene00022766; cblc-1.
DR eggNOG; KOG4552; Eukaryota.
DR GeneTree; ENSGT00390000003464; -.
DR HOGENOM; CLU_095722_0_0_1; -.
DR InParanoid; Q7Z144; -.
DR OMA; QMEVIAD; -.
DR OrthoDB; 1375709at2759; -.
DR PhylomeDB; Q7Z144; -.
DR Reactome; R-CEL-9759218; Cobalamin (Cbl) metabolism.
DR PRO; PR:Q7Z144; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00022766; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031419; F:cobalamin binding; IDA:WormBase.
DR GO; GO:0033787; F:cyanocobalamin reductase (cyanide-eliminating) activity; ISS:UniProtKB.
DR GO; GO:0032451; F:demethylase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; ISS:UniProtKB.
DR GO; GO:0070988; P:demethylation; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR CDD; cd12959; MMACHC-like; 1.
DR InterPro; IPR032037; MMACHC.
DR PANTHER; PTHR31457; PTHR31457; 1.
DR Pfam; PF16690; MMACHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..272
FT /note="MMACHC-like protein"
FT /id="PRO_0000076263"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4U1"
FT BINDING 132..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4U1"
FT BINDING 146..148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4U1"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:5UJC"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:5UJC"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5UJC"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5UJC"
FT STRAND 185..196
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5UJC"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:5UJC"
SQ SEQUENCE 272 AA; 31291 MW; CB99BA62BD7DE8E4 CRC64;
MVTEMSHAES IKRVVDQKLS SHEGFESHMF KIGSYNEAVG ESSPFALPYD DSTMALLILS
TPDMFDVAFR KWVVQKTMDF GSFDEVCEMV SSPIQSFLED RLEIMSEKLR KVEENFEILH
DYSMTPQRRP KILMQTCGHV AGAAFYYQPC HFQEDGVTWP PAGRMGPNLK FIGLSLHPIY
GGHFAFRSVL IFPNVKIPEF CEKEPRPILT ASEDVRTALE KFNYNWKDSG FRDFGNPTRR
YSTTQMEFFG RPVAERWEVL RPWVDGGAKN ID
