DHD2_LACPA
ID DHD2_LACPA Reviewed; 333 AA.
AC P17584;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=D-2-hydroxyisocaproate dehydrogenase;
DE Short=D-HICDH;
DE EC=1.1.1.-;
OS Lacticaseibacillus paracasei (Lactobacillus paracasei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 25598 / DSM 20008 / BCRC 12193 / JCM 1181 / NCDO 2743 / NCIMB
RC 9713 / 40;
RX PubMed=2504649; DOI=10.1016/0378-1119(89)90313-2;
RA Lerch H.-P., Bloecker H., Kallwass H., Hoppe J., Tsai H., Collins J.;
RT "Cloning, sequencing and expression in Escherichia coli of the D-2-
RT hydroxyisocaproate dehydrogenase gene of Lactobacillus casei.";
RL Gene 78:47-57(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NAD AND
RP 2-OXOISOCAPROATE, SEQUENCE REVISION TO 322-333, MASS SPECTROMETRY, AND
RP SUBUNIT.
RC STRAIN=ATCC 25598 / DSM 20008 / BCRC 12193 / JCM 1181 / NCDO 2743 / NCIMB
RC 9713 / 40;
RX PubMed=9126843; DOI=10.1006/jmbi.1996.0864;
RA Dengler U., Niefind K., Kiess M., Schomburg D.;
RT "Crystal structure of a ternary complex of D-2-hydroxyisocaproate
RT dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9-A
RT resolution.";
RL J. Mol. Biol. 267:640-660(1997).
CC -!- FUNCTION: Catalyzes the NAD dependent reversible, stereospecific
CC interconversion between 2-ketocarboxylic acids and D-2-hydroxy-
CC carboxylic acids.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9126843}.
CC -!- MASS SPECTROMETRY: Mass=36880; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9126843};
CC -!- MISCELLANEOUS: Can be applied in an industrial process for the
CC production of D-amino acid.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26929; AAA25236.1; -; Genomic_DNA.
DR PIR; JU0050; DELBC.
DR RefSeq; WP_003577354.1; NZ_VTYT01000003.1.
DR PDB; 1DXY; X-ray; 1.86 A; A=1-333.
DR PDBsum; 1DXY; -.
DR AlphaFoldDB; P17584; -.
DR SMR; P17584; -.
DR DrugBank; DB03229; alpha-Ketoisocaproic acid.
DR BRENDA; 1.1.1.345; 2884.
DR EvolutionaryTrace; P17584; -.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..333
FT /note="D-2-hydroxyisocaproate dehydrogenase"
FT /id="PRO_0000075940"
FT ACT_SITE 234
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 263
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 155..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT BINDING 205..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT BINDING 232..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9126843,
FT ECO:0007744|PDB:1DXY"
FT CONFLICT 322..333
FT /note="GETSTEVTGPAK -> FKPARKLLVQQVVN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1DXY"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:1DXY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1DXY"
FT HELIX 301..321
FT /evidence="ECO:0007829|PDB:1DXY"
SQ SEQUENCE 333 AA; 36893 MW; 40C165872884328B CRC64;
MKIIAYGARV DEIQYFKQWA KDTGNTLEYH TEFLDENTVE WAKGFDGINS LQTTPYAAGV
FEKMHAYGIK FLTIRNVGTD NIDMTAMKQY GIRLSNVPAY SPAAIAEFAL TDTLYLLRNM
GKVQAQLQAG DYEKAGTFIG KELGQQTVGV MGTGHIGQVA IKLFKGFGAK VIAYDPYPMK
GDHPDFDYVS LEDLFKQSDV IDLHVPGIEQ NTHIINEAAF NLMKPGAIVI NTARPNLIDT
QAMLSNLKSG KLAGVGIDTY EYETEDLLNL AKHGSFKDPL WDELLGMPNV VLSPHIAYYT
ETAVHNMVYF SLQHLVDFLT KGETSTEVTG PAK
