ID   Y606_STAS1              Reviewed;         318 AA.
AC   Q49ZM5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase SSP0606;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=SSP0606;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE17751.1; -; Genomic_DNA.
DR   RefSeq; WP_002482556.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q49ZM5; -.
DR   SMR; Q49ZM5; -.
DR   GeneID; 66866755; -.
DR   KEGG; ssp:SSP0606; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_9; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000006371; 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   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; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Putative 2-hydroxyacid dehydrogenase SSP0606"
FT                   /id="PRO_0000312192"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  34974 MW;  938DCFD425F8DD03 CRC64;
     MVKVYIAGPI PEVGLNLLKD QGFEVDMYEG TGIIDKETLK QGVKDADALI SLLSTSVDKE
     VIDAANNLKI ITNYGAGFNN VDIDYARQQN IDVTNTPKAS TNSTAELTFA LVLAVARRIP
     EGDKLCRTTG FDGWAPLFFR GREVSGKTIG IIGLGEIGSA VARRAKAFDM NILYTGPHQK
     VDKEREIGAK YVDLETLLKN ADFVTINAAY NPSLHHQIDK AQFEMMKPTS YLINASRGPI
     VHEKALVQAL KDKEIEGAAL DVFEFEPEIN DELKTLDNVV ITPHIGNATF ESRDMMSKIV
     ANDTISKLNN DQPKFIVN
//