ID   DDH_ZYMMO               Reviewed;         331 AA.
AC   P30799; Q5NN49;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=2-hydroxyacid dehydrogenase homolog;
DE            EC=1.1.1.-;
GN   Name=ddh; Synonyms=ldhA; OrderedLocusNames=ZMO1237;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=8320209; DOI=10.1128/jb.175.13.3926-3933.1993;
RA   Yomano L.P., Scopes R.K., Ingram L.O.;
RT   "Cloning, sequencing, and expression of the Zymomonas mobilis
RT   phosphoglycerate mutase gene (pgm) in Escherichia coli.";
RL   J. Bacteriol. 175:3926-3933(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; L09650; AAA71934.1; -; Genomic_DNA.
DR   EMBL; L09651; AAA71938.1; -; Unassigned_DNA.
DR   EMBL; AE008692; AAV89861.1; -; Genomic_DNA.
DR   PIR; D40649; D40649.
DR   RefSeq; WP_011241053.1; NZ_CP035711.1.
DR   AlphaFoldDB; P30799; -.
DR   SMR; P30799; -.
DR   STRING; 264203.ZMO1237; -.
DR   EnsemblBacteria; AAV89861; AAV89861; ZMO1237.
DR   GeneID; 58027006; -.
DR   KEGG; zmo:ZMO1237; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_5; -.
DR   OMA; VIVTAHQ; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000001173; Chromosome.
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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..331
FT                   /note="2-hydroxyacid dehydrogenase homolog"
FT                   /id="PRO_0000076020"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        297
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         234..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         297..300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        184
FT                   /note="K -> E (in Ref. 1; AAA71934)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="E -> G (in Ref. 1; AAA71934)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   331 AA;  36496 MW;  CFEBF136F9FCC4C4 CRC64;
     MRVAIFSSKN YDHHSIEKEN EHYGHDLVFL NERLTKETAE KAKDAEAVCI FVNDEANAEV
     LEILAGLGIK LVALRCAGYN NVDLDAAKKL NIKVVRVPAY SPYSVAEYAV GMLLTLNRQI
     SRGLKRVREN NFSLEGLIGL DVHDKTVGII GVGHIGSVFA HIMTHGFGAN VIAYKPHPDP
     ELAKKVGFRF TSLDEVIETS DIISLHCPLT PENHHMINEE TLARAKKGFY LVNTSRGGLV
     DTKAVIKSLK AKHLGGYAAD VYEEEGPLFF ENHADDIIED DILERLIAFP NVVFTGHQAF
     LTKEALSNIA HSILQDISDA EAGKEMPDAL V