LADH_METJA
ID LADH_METJA Reviewed; 463 AA.
AC Q58806;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lactaldehyde dehydrogenase;
DE EC=1.2.1.22;
GN OrderedLocusNames=MJ1411;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16585745; DOI=10.1128/jb.188.8.2836-2844.2006;
RA Grochowski L.L., Xu H., White R.H.;
RT "Identification of lactaldehyde dehydrogenase in Methanocaldococcus
RT jannaschii and its involvement in production of lactate for F420
RT biosynthesis.";
RL J. Bacteriol. 188:2836-2844(2006).
CC -!- FUNCTION: Involved in F420 biosynthesis through the oxidation of
CC lactaldehyde to lactate. The substrate preference order is
CC propionaldehyde > DL-lactaldehyde, DL-glyceraldehyde > crotonaldehyde >
CC glycolaldehyde > acetaldehyde, acrolein > formaldehyde. No activity was
CC observed towards methylglyoxal or glyceraldehyde-3-phosphate. Has a
CC preference for NAD over NADP. {ECO:0000269|PubMed:16585745}.
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 Evidence={ECO:0000269|PubMed:16585745};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=284 uM for propionaldehyde (at pH 7.5)
CC {ECO:0000269|PubMed:16585745};
CC KM=302 uM for DL-lactaldehyde (at pH 7.5)
CC {ECO:0000269|PubMed:16585745};
CC Vmax=1.12 umol/min/mg enzyme with propionaldehyde as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:16585745};
CC Vmax=0.6 umol/min/mg enzyme with DL-lactaldehyde as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:16585745};
CC Note=As the lactaldehyde used was a mixture of D and L isomers, the
CC kinetic parameters do not reflect the possible stereospecificity of
CC the enzyme.;
CC pH dependence:
CC Optimum pH is 9. The activity remained constant to pH 10.0. Below pH
CC 9, the activity gradually declined, and the enzyme was inactive at pH
CC 6 or below. {ECO:0000269|PubMed:16585745};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16585745}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99418.1; -; Genomic_DNA.
DR PIR; B64476; B64476.
DR RefSeq; WP_010870928.1; NC_000909.1.
DR PDB; 3PQA; X-ray; 1.50 A; A/B/C/D=1-463.
DR PDB; 3RHD; X-ray; 2.20 A; A/B/C/D=1-463.
DR PDBsum; 3PQA; -.
DR PDBsum; 3RHD; -.
DR AlphaFoldDB; Q58806; -.
DR SMR; Q58806; -.
DR STRING; 243232.MJ_1411; -.
DR EnsemblBacteria; AAB99418; AAB99418; MJ_1411.
DR GeneID; 1452314; -.
DR KEGG; mja:MJ_1411; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR InParanoid; Q58806; -.
DR OMA; WHKLIEQ; -.
DR OrthoDB; 42527at2157; -.
DR PhylomeDB; Q58806; -.
DR BioCyc; MetaCyc:MON-12177; -.
DR BRENDA; 1.2.1.22; 3260.
DR SABIO-RK; Q58806; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IDA:MENGO.
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; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..463
FT /note="Lactaldehyde dehydrogenase"
FT /id="PRO_0000056600"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT BINDING 220..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3PQA"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 87..110
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3PQA"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 319..334
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3PQA"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:3PQA"
FT STRAND 454..462
FT /evidence="ECO:0007829|PDB:3PQA"
SQ SEQUENCE 463 AA; 51136 MW; 46F265686595B6A5 CRC64;
MFIDGKWINR EDMDVINPYS LEVIKKIPAL SREEAKEAID TAEKYKEVMK NLPITKRYNI
LMNIAKQIKE KKEELAKILA IDAGKPIKQA RVEVERSIGT FKLAAFYVKE HRDEVIPSDD
RLIFTRREPV GIVGAITPFN FPLNLSAHKI APAIATGNVI VHHPSSKAPL VCIELAKIIE
NALKKYNVPL GVYNLLTGAG EVVGDEIVVN EKVNMISFTG SSKVGELITK KAGFKKIALE
LGGVNPNIVL KDADLNKAVN ALIKGSFIYA GQVCISVGMI LVDESIADKF IEMFVNKAKV
LNVGNPLDEK TDVGPLISVE HAEWVEKVVE KAIDEGGKLL LGGKRDKALF YPTILEVDRD
NILCKTETFA PVIPIIRTNE EEMIDIANST EYGLHSAIFT NDINKSLKFA ENLEFGGVVI
NDSSLFRQDN MPFGGVKKSG LGREGVKYAM EEMSNIKTII ISK
