GenomeNet

Database: UniProt
Entry: W5MX68_LEPOC
LinkDB: W5MX68_LEPOC
Original site: W5MX68_LEPOC 
ID   W5MX68_LEPOC            Unreviewed;       265 AA.
AC   W5MX68;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Cyanocobalamin reductase / alkylcobalamin dealkylase {ECO:0000256|ARBA:ARBA00014027};
DE            EC=1.16.1.6 {ECO:0000256|ARBA:ARBA00012666};
DE            EC=2.5.1.151 {ECO:0000256|ARBA:ARBA00012308};
DE   AltName: Full=Alkylcobalamin:glutathione S-alkyltransferase {ECO:0000256|ARBA:ARBA00032650};
DE   AltName: Full=CblC {ECO:0000256|ARBA:ARBA00031815};
DE   AltName: Full=Cyanocobalamin reductase (cyanide-eliminating) {ECO:0000256|ARBA:ARBA00031313};
DE   AltName: Full=Methylmalonic aciduria and homocystinuria type C protein {ECO:0000256|ARBA:ARBA00031056};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012977.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012977.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 cob(II)alamin-[cyanocobalamin reductase] + 2 hydrogen
CC         cyanide + NADP(+) = 2 apo-[cyanocobalamin reductase] + 2
CC         cyanocob(III)alamin + H(+) + NADPH; Xref=Rhea:RHEA:16113, Rhea:RHEA-
CC         COMP:14717, Rhea:RHEA-COMP:14718, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16304, ChEBI:CHEBI:17439, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83228; EC=1.16.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00029314};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16115;
CC         Evidence={ECO:0000256|ARBA:ARBA00029314};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)alamin + apo-[alkylcobalamin reductase] +
CC         glutathione = cob(I)alamin-[alkylcobalamin reductase] + H(+) + S-
CC         adenosylglutathione; Xref=Rhea:RHEA:63136, Rhea:RHEA-COMP:14730,
CC         Rhea:RHEA-COMP:14731, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:60488, ChEBI:CHEBI:83228,
CC         ChEBI:CHEBI:146184; EC=2.5.1.151;
CC         Evidence={ECO:0000256|ARBA:ARBA00029328};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63137;
CC         Evidence={ECO:0000256|ARBA:ARBA00029328};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an R-cob(III)alamin + apo-[alkylcobalamin reductase] +
CC         glutathione = an S-substituted glutathione + cob(I)alamin-
CC         [alkylcobalamin reductase] + H(+); Xref=Rhea:RHEA:40719, Rhea:RHEA-
CC         COMP:14730, Rhea:RHEA-COMP:14731, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:60488, ChEBI:CHEBI:83228,
CC         ChEBI:CHEBI:90779, ChEBI:CHEBI:140785; EC=2.5.1.151;
CC         Evidence={ECO:0000256|ARBA:ARBA00029309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40720;
CC         Evidence={ECO:0000256|ARBA:ARBA00029309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[alkylcobalamin reductase] + glutathione +
CC         methylcob(III)alamin = cob(I)alamin-[alkylcobalamin reductase] + H(+)
CC         + S-methyl glutathione; Xref=Rhea:RHEA:63132, Rhea:RHEA-COMP:14730,
CC         Rhea:RHEA-COMP:14731, ChEBI:CHEBI:15378, ChEBI:CHEBI:28115,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:60488, ChEBI:CHEBI:83228,
CC         ChEBI:CHEBI:141467; EC=2.5.1.151;
CC         Evidence={ECO:0000256|ARBA:ARBA00029317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63133;
CC         Evidence={ECO:0000256|ARBA:ARBA00029317};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the MMACHC family.
CC       {ECO:0000256|ARBA:ARBA00007762}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AHAT01000181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MX68; -.
DR   STRING; 7918.ENSLOCP00000012977; -.
DR   Ensembl; ENSLOCT00000013004.1; ENSLOCP00000012977.1; ENSLOCG00000010596.1.
DR   eggNOG; KOG4552; Eukaryota.
DR   GeneTree; ENSGT00390000003464; -.
DR   HOGENOM; CLU_095722_0_0_1; -.
DR   InParanoid; W5MX68; -.
DR   OMA; SDPVDQC; -.
DR   Proteomes; UP000018468; Linkage group LG10.
DR   Bgee; ENSLOCG00000010596; Expressed in ovary and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0033787; F:cyanocobalamin reductase (cyanide-eliminating) activity; IBA:GO_Central.
DR   GO; GO:0032451; F:demethylase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0009235; P:cobalamin metabolic process; IBA:GO_Central.
DR   CDD; cd12959; MMACHC-like; 1.
DR   InterPro; IPR032037; MMACHC.
DR   PANTHER; PTHR31457:SF2; CYANOCOBALAMIN REDUCTASE _ ALKYLCOBALAMIN DEALKYLASE; 1.
DR   PANTHER; PTHR31457; METHYLMALONIC ACIDURIA AND HOMOCYSTINURIA TYPE C PROTEIN; 1.
DR   Pfam; PF16690; MMACHC; 1.
PE   3: Inferred from homology;
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00022628};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   REGION          246..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  29606 MW;  72BA65D3BE3A96DC CRC64;
     MAESGSNVEI VEGRLREVLT PLGFEVYPLQ VGWYNAVLPP SLHLGHPSDT LAAVVLSAPA
     MFESSFLPFL RSQACGSVRD PIDQCVAHYL PRAVAQCFPG QQVEISYDYE MLPNRKPKFL
     AQTAAHVAGA AYYYQQRDVA DNPWGNKKMF GVCVHPRFGG WFAIRALLVF PGVGAAGLEQ
     RDPPDCVPTR EDRIRLLERF NTCWQDWSYR DVVAPAERYS EKQRAYFSAR PADRLALLRD
     WGLLRSEDPG QRASPTPAEP GSHKG
//
DBGET integrated database retrieval system