ID   DDH_HAEIN               Reviewed;         331 AA.
AC   P44501;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=2-hydroxyacid dehydrogenase homolog;
DE            EC=1.1.1.-;
GN   Name=ddh; OrderedLocusNames=HI_0085;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21763.1; -; Genomic_DNA.
DR   PIR; F64047; F64047.
DR   RefSeq; NP_438258.1; NC_000907.1.
DR   RefSeq; WP_005693834.1; NC_000907.1.
DR   AlphaFoldDB; P44501; -.
DR   SMR; P44501; -.
DR   STRING; 71421.HI_0085; -.
DR   EnsemblBacteria; AAC21763; AAC21763; HI_0085.
DR   KEGG; hin:HI_0085; -.
DR   PATRIC; fig|71421.8.peg.86; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_6; -.
DR   OMA; VIVTAHQ; -.
DR   PhylomeDB; P44501; -.
DR   BioCyc; HINF71421:G1GJ1-86-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; 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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..331
FT                   /note="2-hydroxyacid dehydrogenase homolog"
FT                   /id="PRO_0000076021"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         295..298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  37088 MW;  AB13300E94962566 CRC64;
     MKIAIYSTKS YDRKYIELIN AKYNFDLEFF DFMLNESTVR LAEHCEVVCI FVNDNGSRKV
     LEKLAALGVK IVALRCAGFN NVDLKAAQEL GIQVVRVPAY SPEAVAEHTI GLMMTLNRRI
     HRAYQRTREA NFSLEGLIGF NMYGRTVGVI GTGKIGIAVM RILKGFGMNI LAYDPFKNPV
     VEELGGQYVE LDELYAKSHV ITLHCPATPE NYHLLNCEAF AKMKDGVMIV NTSRGSLIDT
     QAAIDALKQR KIGALGMDVY ENERDLFFED KSNEVIQDDI FRRLSSCHNV LLTGHQAFLT
     EEALTNIADV TLSNIYKLKS GKVCENIVLP S