ID   LADH_METMP              Reviewed;         465 AA.
AC   Q6LX65;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Lactaldehyde dehydrogenase;
DE            EC=1.2.1.22;
GN   OrderedLocusNames=MMP1487;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Involved in F420 biosynthesis through the oxidation of
CC       lactaldehyde to lactate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactaldehyde + H2O + NAD(+) = (S)-lactate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:14277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:18041, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.22;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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; BX950229; CAF31043.1; -; Genomic_DNA.
DR   RefSeq; WP_011171431.1; NC_005791.1.
DR   AlphaFoldDB; Q6LX65; -.
DR   SMR; Q6LX65; -.
DR   STRING; 267377.MMP1487; -.
DR   EnsemblBacteria; CAF31043; CAF31043; MMP1487.
DR   GeneID; 2762736; -.
DR   KEGG; mmp:MMP1487; -.
DR   PATRIC; fig|267377.15.peg.1523; -.
DR   eggNOG; arCOG01252; Archaea.
DR   HOGENOM; CLU_005391_1_0_2; -.
DR   OMA; WHKLIEQ; -.
DR   OrthoDB; 42527at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07645-MON; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..465
FT                   /note="Lactaldehyde dehydrogenase"
FT                   /id="PRO_0000342592"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         220..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  50981 MW;  A70FE58C9B30D8A2 CRC64;
     MFIDGKWIIR EDIDVFDPYT LENIEKITAL DREETKNAIE VTEKHKEIMK NLSPSKRYKI
     LMKVAEHLSS KKDFFAKTIS IDVGKPIKQS KIEVDRTLTA LKLSAFYAKE LRGETINSEN
     GLIFTKKEPL GVIGAITPFN FPLNLATHKI GPAIATGNSV VLHPSSKAPI VAIYLTKIIE
     HVLKQMDIPR GVFNLATGNG EIVGDEISKN DNVNMVSFTG SVEVGESISK NAKMKKVTLE
     LGGNNPMIVL KDSDIKLAAK SAVKSKFLNA GQVCISVGQV LVEEEVVETF TKYVIEETKK
     LILGNPLDKN TDIGPLISPE SALRIENLIK QSVSEGGELL IGGNRQNSLI SPAVINIDEE
     NILSKIETFG PILPILTVKD SEEAVNIANN SKYGLQAGLF TNNINNAMKI ADELEYGGIM
     INSSPTFRKD NMPFGGVKKS GLGREGIKYT VEEMSETKTV VIHNI