ID F3ZUA4_9BACE Unreviewed; 318 AA.
AC F3ZUA4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:EGJ71349.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:EGJ71349.1};
GN ORFNames=Bcop_1145 {ECO:0000313|EMBL:EGJ71349.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ71349.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ71349.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ71349.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CM001167; EGJ71349.1; -; Genomic_DNA.
DR RefSeq; WP_006744506.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZUA4; -.
DR STRING; 679937.Bcop_1145; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_10; -.
DR OrthoDB; 9777288at2; -.
DR Proteomes; UP000018439; Chromosome.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000018439}.
FT DOMAIN 22..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 35502 MW; 6D61782FD905A6F2 CRC64;
MKIVILDGYA ANPGDLEWDG LEQLGDCTLY DRTSRDQVLE RCKDANIVLT NKVPFKRETI
EALPNLKYIG VMATGYNIID TEAAKEKGIV VTNIPSYSTN SVAQMVFAHI LNITLHVQKH
SDEVHQGRWS KNADFCFWDS PLLELHGRTI GIIGLGSIGQ AVARIAFGFG MKVIAYTSKT
QLQLPHEIQK VELDELFEQA DIVTLHCPLT DETRNMVDKR RLELMQPTSI IINTSRGPLI
NEADLAEALK NKTIYAAGID VMSQEPPKAD NPLLGVENCY ITPHIAWASF AARTRLMKIL
INNVKAFMEG KPENQVNK
//
