ID   DLAG_AMYME              Reviewed;          21 AA.
AC   P80414;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=DYE-linked aldehyde dehydrogenase, gamma chain;
DE            Short=DL-ALDH;
DE            EC=1.2.99.-;
DE   Flags: Fragment;
OS   Amycolatopsis methanolica.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1814;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND COFACTOR.
RC   STRAIN=DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946 / NRRL B-24139 / LMD
RC   80.32 / 239;
RX   PubMed=8554333; DOI=10.1006/abbi.1996.0001;
RA   Kim S.W., Luykx D.M.A.M., de Vries S., Duine J.A.;
RT   "A second molybdoprotein aldehyde dehydrogenase from Amycolatopsis
RT   methanolica NCIB 11946.";
RL   Arch. Biochem. Biophys. 325:1-7(1996).
CC   -!- FUNCTION: Active with aldehydes and formate esters as substrates.
CC       {ECO:0000269|PubMed:8554333}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:8554333};
CC       Note=Binds 2 [2Fe-2S] clusters per subunit.
CC       {ECO:0000269|PubMed:8554333};
CC   -!- SUBUNIT: Heterotetramer composed of an alpha, a beta and two gamma
CC       chains.
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DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..>21
FT                   /note="DYE-linked aldehyde dehydrogenase, gamma chain"
FT                   /id="PRO_0000079927"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2315 MW;  9AA9E314DD945772 CRC64;
     MKVSIEINGT TVSXEVXDRT L