GenomeNet

Database: UniProt
Entry: D1C3Y3_SPHTD
LinkDB: D1C3Y3_SPHTD
Original site: D1C3Y3_SPHTD 
ID   D1C3Y3_SPHTD            Unreviewed;       316 AA.
AC   D1C3Y3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ACZ38950.1};
GN   OrderedLocusNames=Sthe_1515 {ECO:0000313|EMBL:ACZ38950.1};
OS   Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC   Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX   NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ38950.1, ECO:0000313|Proteomes:UP000002027};
RN   [1] {ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA   Goeker M., Klenk H.P., Eisen J.A.;
RT   "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ38950.1, ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA   Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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; CP001823; ACZ38950.1; -; Genomic_DNA.
DR   RefSeq; WP_012871997.1; NC_013523.1.
DR   AlphaFoldDB; D1C3Y3; -.
DR   STRING; 479434.Sthe_1515; -.
DR   KEGG; sti:Sthe_1515; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_0; -.
DR   InParanoid; D1C3Y3; -.
DR   OrthoDB; 9792971at2; -.
DR   Proteomes; UP000002027; Chromosome 1.
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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12173; PGDH_4; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002027}.
FT   DOMAIN          9..312
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..280
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   316 AA;  33575 MW;  78F4A43B89B1D4EB CRC64;
     MEGAGQPRIL VCDPIDDGAL DLLRRHARVD VRTSLAPDEL VDIVGGYDGL VVRGTTQITS
     EVIEAATALR GIARVGFAVD NIDIDAATER GIVVVHSPGA RTYAVAEMTI GLILAVLRHI
     PAADRSVKAG RWERRAFRGR QLRGATVGVI GYGRIGREVA RLAHAFGATV KAYTQTPRPL
     EHAKQVDFQA LLASSDIITL HATLTSATRQ LINREAIEQM RDGVVIVNTA SGGLIDEAAL
     LEALDRGKVA GAGLDVFADE PPSLRALVEH PRVVTTPRIG GSTQEADRAV SELALQSLLA
     VLRGEQPAVA VNPQGR
//
DBGET integrated database retrieval system