ID LADH_METM5 Reviewed; 465 AA.
AC A4FW36;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Lactaldehyde dehydrogenase;
DE EC=1.2.1.22;
GN OrderedLocusNames=MmarC5_0090;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000609; ABO34407.1; -; Genomic_DNA.
DR RefSeq; WP_011867868.1; NC_009135.1.
DR AlphaFoldDB; A4FW36; -.
DR SMR; A4FW36; -.
DR STRING; 402880.MmarC5_0090; -.
DR GeneID; 4928313; -.
DR KEGG; mmq:MmarC5_0090; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR OrthoDB; 6342at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000253; Chromosome.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd07145; ALDH_LactADH_F420-Bios; 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 NCBIfam; NF040648; lactal_redase_Meth; 1.
DR PANTHER; PTHR42991; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42991:SF1; ALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..465
FT /note="Lactaldehyde dehydrogenase"
FT /id="PRO_0000342590"
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; 50803 MW; 37DC771138E8154A CRC64;
MFIDGKWILR EDIDVFDPYT LENIEKITAL DREETKSAIE VAEKNKEIMK NLSPSKRYSI
LMKIAEQISL KKDLFAKTIS IDVGKPIKQS KIEVDRTLTA LKLSAFYAKE LRGETINSEN
GLIFTKKEPL GVVGAITPFN FPLNLITHKI GPAIATGNSV VLHPSSKAPI VAIYLTKIIE
HVLKQMDVPR GIFNLATGNG DIVGDEISKN DNINMVSFTG SVEVGESISK NAKMKKVALE
LGGNNPMIVL KDSDIKLAAK SAVKSKFLNA GQVCISVGQV LVEEEVLETF TKHVIEETKK
LILGNPLDTK TDIGPLISPE SALRIENLIK KSVNEGGEVL IGGNRQNSLI SPAVINIDEN
NILSKIETFG PVLPILKVKD SEEAVSIANN SKYGLQAGVF TNDINKAMKI ADSLEYGGIM
INSSPTFRKD NMPFGGVKKS GLGREGIKYT VEEMCETKTI VIHNI
//
