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Database: UniProt
Entry: A0A2K6FLI0_PROCO
LinkDB: A0A2K6FLI0_PROCO
Original site: A0A2K6FLI0_PROCO 
ID   A0A2K6FLI0_PROCO        Unreviewed;       282 AA.
AC   A0A2K6FLI0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
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};
GN   Name=MMACHC {ECO:0000313|Ensembl:ENSPCOP00000014833.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000014833.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000014833.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_012504419.1; XM_012648965.1.
DR   AlphaFoldDB; A0A2K6FLI0; -.
DR   STRING; 379532.ENSPCOP00000014833; -.
DR   Ensembl; ENSPCOT00000025443.1; ENSPCOP00000014833.1; ENSPCOG00000019121.1.
DR   GeneID; 105814081; -.
DR   KEGG; pcoq:105814081; -.
DR   CTD; 25974; -.
DR   GeneTree; ENSGT00390000003464; -.
DR   OMA; SDPVDQC; -.
DR   OrthoDB; 3035512at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0033787; F:cyanocobalamin reductase (cyanide-eliminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0032451; F:demethylase activity; IEA:Ensembl.
DR   GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR   GO; GO:0043295; F:glutathione binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0009235; P:cobalamin metabolic process; IEA:Ensembl.
DR   GO; GO:0070988; P:demethylation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
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:UP000233160}.
FT   REGION          237..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  31818 MW;  81360831DAB8EB50 CRC64;
     MEPRVAELKQ KIEDTLCPFG FEVYPFQVAW YNELLPPAFH LPLPGPTLAF LVLSTPAMFD
     RALKPFLQSC HLQLLTDPVD QCVAYHLNRV RESLPELQIE VIADYEVHHN RRPKILVQTA
     AHVAGAAYYY QRQDVEADPW GTQHISGVCI HPRFGGWFAI RGVVLLPGIE VPDLPPRKPP
     DCVPTRADRI ALLEGFNFHW RDWTYRDAVT PQERYSEEQK AYFSTPPSQR LALLGLTQPS
     EKPSSLSPDL PFTTLTSKKP QNPSKARGWL NPSVSPPASP GP
//
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