LADH_METVS
ID LADH_METVS Reviewed; 465 AA.
AC A6UQD0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Lactaldehyde dehydrogenase;
DE EC=1.2.1.22;
GN OrderedLocusNames=Mevan_0796;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-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; CP000742; ABR54702.1; -; Genomic_DNA.
DR RefSeq; WP_011972604.1; NC_009634.1.
DR AlphaFoldDB; A6UQD0; -.
DR SMR; A6UQD0; -.
DR STRING; 406327.Mevan_0796; -.
DR EnsemblBacteria; ABR54702; ABR54702; Mevan_0796.
DR GeneID; 5324651; -.
DR KEGG; mvn:Mevan_0796; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR OMA; WHKLIEQ; -.
DR OrthoDB; 42527at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001107; 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.
FT CHAIN 1..465
FT /note="Lactaldehyde dehydrogenase"
FT /id="PRO_0000342593"
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; 51019 MW; DDDDAE5D57893F99 CRC64;
MFIDGKWILR EDLDILNPYT LEIIERITAL DREETKYAIE VATENKDVMK ELNPSKRYSL
LMKIAEHISS KKDLFANTIS VDVGKPIKQS RIEVDRTITA FRLSALYAKE LRGETIPSEN
EIIFTKKEPV GVVGAITPFN FPLNLITHKI GPAIATGNAV VLHPSSKAPI TAIYLTKVIE
HVLKKMNIER GVFNLTTGNG EIVGDEIAKN EKINFLSFTG SVEVGELISK SSYMKKVALE
LGGNNPLIVL KDSDIELAAK SAVKSKFLNS GQVCISVGKV IVEEEVLETF TKKVIEETKK
LVLGNPLDEK TDLGPLITPE SALRVEILIK ESISEGGELL IGGNRSNSLI SPAVLNIDED
NILSKVEAFG PILPILKAKD DEHALNIANN SKYGLQAGIF TNDINKAMKF ANKLEYGGVI
VNGSPTFRKD NMPFGGIKKS GLGKEGIKYA VEEMCETKTV VIHNM