ID A0A0B4Y278_9PROT Unreviewed; 315 AA.
AC A0A0B4Y278;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:AJD53325.1};
GN ORFNames=TH3_16115 {ECO:0000313|EMBL:AJD53325.1};
OS Thalassospira xiamenensis M-5 = DSM 17429.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1123366 {ECO:0000313|EMBL:AJD53325.1, ECO:0000313|Proteomes:UP000007127};
RN [1] {ECO:0000313|EMBL:AJD53325.1, ECO:0000313|Proteomes:UP000007127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M-5 {ECO:0000313|EMBL:AJD53325.1,
RC ECO:0000313|Proteomes:UP000007127};
RX PubMed=23209216; DOI=10.1128/JB.01904-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of Thalassospira xiamenensis type strain M-5.";
RL J. Bacteriol. 194:6957-6957(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP004388; AJD53325.1; -; Genomic_DNA.
DR RefSeq; WP_007089804.1; NZ_FTON01000017.1.
DR AlphaFoldDB; A0A0B4Y278; -.
DR STRING; 1123366.TH3_16115; -.
DR GeneID; 31928895; -.
DR KEGG; txi:TH3_16115; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR Proteomes; UP000007127; 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; cd12156; HPPR; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 8..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 33615 MW; 3A4B9A48077F8EAE CRC64;
MSRSDKHILV ISAIRPRHME ELAAKYELHR WDQATDKDAF LANVADRITA LVSTAGVGVP
TELIGKLPNL KVITSFGVGY DAIDIAACTA RGIRVSNTPD VLNDDVADTA IMLLLATLRR
LVVGDHWARS GQWSEKGAMP LTTTARGKKL GIVGLGRIGQ AIAARAEPIG MEIGYFGRSK
KPVDYHYEAD LIGLANWADV LMVSCPGGAA TQGIINADVL KALGPRGFVI NIARGSVIDE
PALIAALRDG VIAGAGLDVF HNEPHMDRAF AGFDNVVLYP HNASGTVETR DAMAQMVVDN
LAQWFADGTL VSPVN
//
