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Database: UniProt
Entry: A0A1H8P3L2_9RHOB
LinkDB: A0A1H8P3L2_9RHOB
Original site: A0A1H8P3L2_9RHOB 
ID   A0A1H8P3L2_9RHOB        Unreviewed;       335 AA.
AC   A0A1H8P3L2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:SEO36427.1};
GN   ORFNames=SAMN04489859_10794 {ECO:0000313|EMBL:SEO36427.1};
OS   Paracoccus alcaliphilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34002 {ECO:0000313|EMBL:SEO36427.1, ECO:0000313|Proteomes:UP000199054};
RN   [1] {ECO:0000313|EMBL:SEO36427.1, ECO:0000313|Proteomes:UP000199054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8512 {ECO:0000313|EMBL:SEO36427.1,
RC   ECO:0000313|Proteomes:UP000199054};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FODE01000079; SEO36427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8P3L2; -.
DR   STRING; 34002.SAMN04489859_10794; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000199054; Unassembled WGS sequence.
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; cd05301; GDH; 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; 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   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199054}.
FT   DOMAIN          20..330
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          120..299
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   335 AA;  36963 MW;  ADB35C63DE3F3140 CRC64;
     MSSNPSSPAR QRLRISVTRR LPETVETRMS ELFDVSLNES DRRMSRDELV VAMQNCDVLV
     PTVTDHIDAN MLAQAGGRLK LIANYGAGVD HIDVLSARQR GILVSNTPGV VTEDTADMVM
     ALILSVTRRI PEGMAEMQAG RWQGWAPTAH LGGRVGGRRL GILGMGRIGQ AVARRANVFG
     MQVHYHNRKR LRPEIEADLQ ATWWESLDQM LARMDIVSVN APHTPSTFHL LNARRLKLLK
     PSAVVVNTSR GEVIDENALT RMLRAGEIAG AGLDVFEHGH EINPRLRELP NVVLLPHMGS
     ATVEGRAEMG EKVIINIKTF DDGHRPPDLV VPSML
//
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