ID A0A0D5M0T2_9GAMM Unreviewed; 307 AA.
AC A0A0D5M0T2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glyoxylate reductase (NADP(+)) {ECO:0000313|EMBL:AJY50014.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:AJY50014.1};
GN ORFNames=KO116_01527 {ECO:0000313|EMBL:AJY50014.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY50014.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY50014.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY50014.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP011052; AJY50014.1; -; Genomic_DNA.
DR RefSeq; WP_035560288.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M0T2; -.
DR STRING; 1504981.KO116_01527; -.
DR KEGG; hak:KO116_01527; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AJY50014.1}.
FT DOMAIN 100..272
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 307 AA; 33849 MW; D3AE6F3629CB3DB1 CRC64;
MSFVYNADPE RGQEWERLFA LHAPDMAFHH WPDYGDPLDV RYLGTWAPIE DLERFSNLEV
IFSLGAGVDQ FDLDALPHHV PLVRMQEPGI VATMQAYVAM AVLGLHRDLL SYIAQQRERV
WKTWRVRPAA QCCVGILGLG QLGAAVAQHL VGLGFSCRGW SRTARELPGV KCYAGEAALG
DFLAGSDILV CLLPLTDHTR GILDARLFAQ LPRGASLINV GRGAHLVDRD LLSALDSGQL
SAAVLDVFAP EPPPADHPLW HHPRVLLTPH VASMTQPESA VMMLLDNIAR HQAGHEMMGV
VDRKRGY
//