LADH_METM7
ID LADH_METM7 Reviewed; 465 AA.
AC A6VH72;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Lactaldehyde dehydrogenase;
DE EC=1.2.1.22;
GN OrderedLocusNames=MmarC7_0731;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR65798.1; -; Genomic_DNA.
DR RefSeq; WP_011977118.1; NC_009637.1.
DR AlphaFoldDB; A6VH72; -.
DR SMR; A6VH72; -.
DR STRING; 426368.MmarC7_0731; -.
DR EnsemblBacteria; ABR65798; ABR65798; MmarC7_0731.
DR GeneID; 5327882; -.
DR KEGG; mmz:MmarC7_0731; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR OMA; GMKYVTM; -.
DR OrthoDB; 42527at2157; -.
DR UniPathway; UPA00071; -.
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_0000342591"
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; 51010 MW; 6E7A60209265F421 CRC64;
MFIDGKWIIR DDIDVFDPYT LKNIEKITAL DREETKNAIE ITEKNKEVMK NLSPSKRYSI
LMKIAEQISL KKDLFAKTIS IDVGKPIKQS KIEVDRTLTA FRLSAFYAKE LRGETINSEN
GLIFTKKEPL GVVGAITPFN FPLNLITHKI GPAIATGNSV ILHPSSKAPI AAIYLTKIIE
HVLKQMDIPR GVFNLATGNG DIVGDEISKN DKINMVSFTG SVEIGESISK NAKMKKVTLE
LGGNNPMIVL KDSDIKLAAK SAVKSKFLNA GQVCISVGQV LVEEEVLETF TKYIIDETKN
LVLGNPLDTK TDIGPLISPE SALRIENLIK ESVNEGGELL IGGNRQNSLI FPAVINIDED
NLLSKIETFG PVLPILKVKN SEEAVSIANN SKYGLQAGVF TNDINKAMKI ADSLEYGGIM
INSSPTFRKD NMPFGGVKKS GLGREGIKYT VEEMCETKTV VIHNI