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Database: UniProt
Entry: P17584
LinkDB: P17584
Original site: P17584 
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   07-NOV-2018, entry version 105.
DE   RecName: Full=D-2-hydroxyisocaproate dehydrogenase;
DE            Short=D-HICDH;
DE            EC=1.1.1.-;
OS   Lactobacillus paracasei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25598 / DSM 20008 / JCM 1181 / NCDO 2743 / NCIMB 9713;
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 / JCM 1181 / NCDO 2743 / NCIMB 9713;
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
RT   1.9-A 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; Range=1-333;
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}.
DR   EMBL; M26929; AAA25236.1; -; Genomic_DNA.
DR   PIR; JU0050; DELBC.
DR   RefSeq; WP_003577354.1; NZ_QVHW01000030.1.
DR   PDB; 1DXY; X-ray; 1.86 A; A=1-333.
DR   PDBsum; 1DXY; -.
DR   ProteinModelPortal; P17584; -.
DR   SMR; P17584; -.
DR   DrugBank; DB03229; 2-Oxo-4-Methylpentanoic Acid.
DR   PRIDE; P17584; -.
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       D-2-hydroxyisocaproate dehydrogenase.
FT                                /FTId=PRO_0000075940.
FT   NP_BIND     155    156       NAD. {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   NP_BIND     205    206       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   NP_BIND     232    234       NAD. {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   ACT_SITE    234    234       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    263    263       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    295    295       Proton donor.
FT                                {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     175    175       NAD. {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   BINDING     205    205       NAD; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   BINDING     211    211       NAD. {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   BINDING     258    258       NAD. {ECO:0000244|PDB:1DXY,
FT                                ECO:0000269|PubMed:9126843}.
FT   CONFLICT    322    333       GETSTEVTGPAK -> FKPARKLLVQQVVN (in Ref.
FT                                1). {ECO:0000305}.
FT   STRAND        2      5       {ECO:0000244|PDB:1DXY}.
FT   TURN         10     12       {ECO:0000244|PDB:1DXY}.
FT   HELIX        13     23       {ECO:0000244|PDB:1DXY}.
FT   STRAND       26     29       {ECO:0000244|PDB:1DXY}.
FT   HELIX        38     42       {ECO:0000244|PDB:1DXY}.
FT   STRAND       46     50       {ECO:0000244|PDB:1DXY}.
FT   HELIX        58     66       {ECO:0000244|PDB:1DXY}.
FT   STRAND       71     77       {ECO:0000244|PDB:1DXY}.
FT   HELIX        84     89       {ECO:0000244|PDB:1DXY}.
FT   STRAND       93     95       {ECO:0000244|PDB:1DXY}.
FT   HELIX       102    117       {ECO:0000244|PDB:1DXY}.
FT   HELIX       120    128       {ECO:0000244|PDB:1DXY}.
FT   HELIX       132    135       {ECO:0000244|PDB:1DXY}.
FT   HELIX       143    145       {ECO:0000244|PDB:1DXY}.
FT   STRAND      146    151       {ECO:0000244|PDB:1DXY}.
FT   HELIX       155    166       {ECO:0000244|PDB:1DXY}.
FT   STRAND      170    174       {ECO:0000244|PDB:1DXY}.
FT   HELIX       191    197       {ECO:0000244|PDB:1DXY}.
FT   STRAND      199    203       {ECO:0000244|PDB:1DXY}.
FT   HELIX       209    211       {ECO:0000244|PDB:1DXY}.
FT   HELIX       217    222       {ECO:0000244|PDB:1DXY}.
FT   STRAND      227    231       {ECO:0000244|PDB:1DXY}.
FT   HELIX       240    248       {ECO:0000244|PDB:1DXY}.
FT   STRAND      251    259       {ECO:0000244|PDB:1DXY}.
FT   HELIX       263    273       {ECO:0000244|PDB:1DXY}.
FT   HELIX       279    285       {ECO:0000244|PDB:1DXY}.
FT   STRAND      290    292       {ECO:0000244|PDB:1DXY}.
FT   HELIX       301    321       {ECO:0000244|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
//
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