ID K2JEH6_9RHOB Unreviewed; 328 AA.
AC K2JEH6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glycolate reductase {ECO:0000313|EMBL:EKE69009.1};
GN ORFNames=B30_16713 {ECO:0000313|EMBL:EKE69009.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE69009.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE69009.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE69009.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE69009.1}.
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DR EMBL; AMRK01000011; EKE69009.1; -; Genomic_DNA.
DR RefSeq; WP_009573328.1; NZ_AMRK01000011.1.
DR AlphaFoldDB; K2JEH6; -.
DR STRING; 1208323.B30_16713; -.
DR PATRIC; fig|1208323.3.peg.3463; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000006762; 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:UP000006762}.
FT DOMAIN 9..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 36128 MW; DD70229F999C2939 CRC64;
MVQGRLKVVV TRALPEVVET RMMELFDVEL NQDDVKLSRE ALIAAMQRAD VLVPCVTDRL
DAEMLGQAGE RLKLIANYGA GVDHIDTITA HNRGILVTNT PGVVTEDTAD MVMALILAVT
RRIPEGQAVM QAGNWGGWAP TAFMGQRLSG KRLGILGMGR IGQAVARRAH AFGLSVQYHN
RRRLHPDVEA RFEATYWDSL DQMLSRVDIL SINCPHTPST FHQINARRLK LMKPTAVIVN
TSRGEVIDEN ALTRGLRSGD IGGAGLDVFE HGHQINPRLR ELPNVVLLPH MGSATVEGRI
EMGEKVLLNI HTFADGHRPP DMVLPSML
//
