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Database: UniProt
Entry: A0A3B1JHZ8_ASTMX
LinkDB: A0A3B1JHZ8_ASTMX
Original site: A0A3B1JHZ8_ASTMX 
ID   A0A3B1JHZ8_ASTMX        Unreviewed;       256 AA.
AC   A0A3B1JHZ8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000040929.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000040929.1}
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}.
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DR   AlphaFoldDB; A0A3B1JHZ8; -.
DR   STRING; 7994.ENSAMXP00000040929; -.
DR   Ensembl; ENSAMXT00000048632.1; ENSAMXP00000040929.1; ENSAMXG00000041876.1.
DR   GeneTree; ENSGT00390000003464; -.
DR   InParanoid; A0A3B1JHZ8; -.
DR   OrthoDB; 3035512at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000041876; Expressed in heart and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0033787; F:cyanocobalamin reductase (cyanide-eliminating) activity; IEA:UniProtKB-EC.
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:UP000018467}.
SQ   SEQUENCE   256 AA;  29458 MW;  58F06CFEEB73B68C CRC64;
     MATSSHNVDN VVRTLRESLK TLGFEVYPFK IGWYNAVVSQ AHQLKYSADT LAVVVLSTPS
     MFENSFLPFL QRCSWKDIRD PVDQCVAHAI STCVSEHFSD QSVDISYDYE MQSNRKPKFL
     AQTAAHVAGA ARYYQHTDIE NPPWGNKKMF GVCIHPRLGG WFAIRAVLVW KDVEVGKELQ
     QVPPPDCVSS QEARIKLLEK FNYNWQDWTY RDIVPTEESY STRQREYFIT PPAQRGALLR
     QWGFIPETET KTVNNI
//
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