ID   Y2178_STAAB             Reviewed;         317 AA.
AC   Q2YYT9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SAB2178;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SAB2178;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI81867.1; -; Genomic_DNA.
DR   RefSeq; WP_000417010.1; NC_007622.1.
DR   AlphaFoldDB; Q2YYT9; -.
DR   SMR; Q2YYT9; -.
DR   KEGG; sab:SAB2178; -.
DR   HOGENOM; CLU_019796_1_2_9; -.
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   CDD; cd12178; 2-Hacid_dh_13; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..317
FT                   /note="Putative 2-hydroxyacid dehydrogenase SAB2178"
FT                   /id="PRO_0000312182"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
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         283..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  34689 MW;  49D41FDFA2A10B07 CRC64;
     MEKVYVAGAI PEVGLKLLQE HFEVEMYEGK GLVDKDTLIK GVKNATALIS LLSTNVDKDV
     IDAGKDLKII ANYGAGFNNI DIEYAREKSI DVTNTPKAST NATADLTIGL VLAIARRIVE
     GDQLSRTTGF DGWAPLFFRG REVSGKTIGI IGLGEIGSAV ARRARAFDMD VLYTGPNRKE
     EKEREIGAKY VDLDTLLKNA DFITINAAYN PKMHHLIDTE QFKMMKSTAY LINASRGPIV
     HEQALVQALK DNEIEGAALD VYEFEPDITD DLKSLNNVVL TPHIGNATFE ARDMMSKIVA
     NAAISAVQGE KPQFVVN
//