DHL2_WEICO
ID DHL2_WEICO Reviewed; 310 AA.
AC P14295;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=L-2-hydroxyisocaproate dehydrogenase;
DE Short=L-HicDH;
DE EC=1.1.1.-;
OS Weissella confusa (Lactobacillus confusus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Weissella.
OX NCBI_TaxID=1583;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10881 / DSM 20196 / CCUG 30113 / JCM 1093 / LMG 9497 / NBRC
RC 106469 / NCIMB 9311 / NRRL B-1064 / 548-D;
RX PubMed=2684788; DOI=10.1016/0378-1119(89)90112-1;
RA Lerch H.-P., Frank R., Collins J.;
RT "Cloning, sequencing and expression of the L-2-hydroxyisocaproate
RT dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia
RT coli.";
RL Gene 83:263-270(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-26.
RA Tsai H., Lerch H.-P., Kalwass H., Schuette H., Hoppe J., Collins J.;
RL (In) Neijssel O.M., van der Meer R.R., Luyben K.C.A.M. (eds.);
RL Proceedings 4th European congress biotechnology, pp.2:228-231, Elsevier,
RL Amsterdam (1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD.
RX PubMed=7643402; DOI=10.1006/jmbi.1995.0433;
RA Niefind K., Hecht H.-J., Schomburg D.;
RT "Crystal structure of L-2-hydroxyisocaproate dehydrogenase from
RT Lactobacillus confusus at 2.2-A resolution. An example of strong asymmetry
RT between subunits.";
RL J. Mol. Biol. 251:256-281(1995).
CC -!- FUNCTION: Catalyzes the NADP dependent reversible and stereospecific
CC interconversion between 2-ketocarboxylic acids and L-2-hydroxy-
CC carboxylic acids. 2-ketoacids with medium chain length (five to six C-
CC atoms) are the best substrates.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7643402}.
CC -!- MISCELLANEOUS: Can be applied in an industrial process for the
CC production of L-amino acid.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; M31425; AAA88213.1; -; Genomic_DNA.
DR PIR; JQ0114; JQ0114.
DR RefSeq; WP_003607654.1; NZ_QSBT01000002.1.
DR PDB; 1HYH; X-ray; 2.20 A; A/B/C/D=2-310.
DR PDBsum; 1HYH; -.
DR AlphaFoldDB; P14295; -.
DR SMR; P14295; -.
DR STRING; 1583.IV69_GL001588; -.
DR GeneID; 57979094; -.
DR BRENDA; 1.1.1.337; 2857.
DR SABIO-RK; P14295; -.
DR EvolutionaryTrace; P14295; -.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..310
FT /note="L-2-hydroxyisocaproate dehydrogenase"
FT /id="PRO_0000168501"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10002"
FT BINDING 34..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7643402"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1HYH"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1HYH"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:1HYH"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:1HYH"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1HYH"
FT HELIX 286..307
FT /evidence="ECO:0007829|PDB:1HYH"
SQ SEQUENCE 310 AA; 33180 MW; 947A7FFFB72B5DE7 CRC64;
MARKIGIIGL GNVGAAVAHG LIAQGVADDY VFIDANEAKV KADQIDFQDA MANLEAHGNI
VINDWAALAD ADVVISTLGN IKLQQDNPTG DRFAELKFTS SMVQSVGTNL KESGFHGVLV
VISNPVDVIT ALFQHVTGFP AHKVIGTGTL LDTARMQRAV GEAFDLDPRS VSGYNLGEHG
NSQFVAWSTV RVMGQPIVTL ADAGDIDLAA IEEEARKGGF TVLNGKGYTS YGVATSAIRI
AKAVMADAHA ELVVSNRRDD MGMYLSYPAI IGRDGVLAET TLDLTTDEQE KLLQSRDYIQ
QRFDEIVDTL
