FADH_AMYME
ID FADH_AMYME Reviewed; 360 AA.
AC P80094;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=S-(hydroxymethyl)mycothiol dehydrogenase;
DE EC=1.1.1.306;
DE AltName: Full=NAD/mycothiol-dependent formaldehyde dehydrogenase;
DE Short=MD-FALDH;
OS Amycolatopsis methanolica.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1814;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=9346279; DOI=10.1111/j.1432-1033.1997.00282.x;
RA Norin A., van Ophem P.W., Piersma S.R., Persson B., Duine J.A.,
RA Joernvall H.;
RT "Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain
RT dehydrogenase/reductase, phylogenetically links different eukaroytic
RT alcohol dehydrogenases -- primary structure, conformational modelling and
RT functional correlations.";
RL Eur. J. Biochem. 248:282-289(1997).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 1-31.
RX PubMed=1597190; DOI=10.1111/j.1432-1033.1992.tb16954.x;
RA van Ophem P.W., van Beeumen J., Duine J.A.;
RT "NAD-linked, factor-dependent formaldehyde dehydrogenase or trimeric, zinc-
RT containing, long-chain alcohol dehydrogenase from Amycolatopsis
RT methanolica.";
RL Eur. J. Biochem. 206:511-518(1992).
RN [3]
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=9202149; DOI=10.1016/s0014-5793(97)00510-3;
RA Misset-Smits M., van Ophem P.W., Sakuda S., Duine J.A.;
RT "Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-
RT glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent
RT formaldehyde dehydrogenase.";
RL FEBS Lett. 409:221-222(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)mycothiol = H(+) + NADH + S-
CC formylmycothiol; Xref=Rhea:RHEA:28502, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15735, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61586; EC=1.1.1.306;
CC Evidence={ECO:0000269|PubMed:9202149};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P80094; -.
DR SMR; P80094; -.
DR GO; GO:0050607; F:mycothiol-dependent formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR017816; MycoS_dep_FDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03451; mycoS_dep_FDH; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..360
FT /note="S-(hydroxymethyl)mycothiol dehydrogenase"
FT /id="PRO_0000160786"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 37757 MW; 48BED1F70EAB2CB7 CRC64;
PQTVRGVIAR SKGAPVELTD IVIPDPGPSE VTALIATCAV CHTDLTYREG GINDEFPFLL
GHEAAGTVES VGEGVDSVQP GDYVVLNWRA VCGQCRACKR GRPQYCFSTF NATQKMTLTD
GTELTPALGI GAFADKTLVH AGQCTKVDPA ADPAVAGLLG CGVMAGLGAA VNTGAVSRGD
SVAVIGCGAV GDAVIAGARL AGANKIIAVD RDAKKLEWAT ELGATHTVNA TETDVVEAVQ
ALTGGFGADV VIDAVGRPET WKQAFYARDL AGTVVLVGVP TPDMRLEMPL LDFFSRGGAL
KSSWYGDCLP ERDFPVLIDL HLQGRLPLDK FVTERISLDD VEKAFHTMHA GEVLRSVVVW
