ID G9XWL1_DESHA Unreviewed; 338 AA.
AC G9XWL1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:EHL03963.1};
GN ORFNames=HMPREF0322_05378 {ECO:0000313|EMBL:EHL03963.1};
OS Desulfitobacterium hafniense DP7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL03963.1, ECO:0000313|Proteomes:UP000004416};
RN [1] {ECO:0000313|EMBL:EHL03963.1, ECO:0000313|Proteomes:UP000004416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP7 {ECO:0000313|EMBL:EHL03963.1,
RC ECO:0000313|Proteomes:UP000004416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHL03963.1}.
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DR EMBL; AFZX01000140; EHL03963.1; -; Genomic_DNA.
DR RefSeq; WP_005817430.1; NZ_JH414492.1.
DR AlphaFoldDB; G9XWL1; -.
DR PATRIC; fig|537010.4.peg.5012; -.
DR HOGENOM; CLU_019796_1_2_9; -.
DR Proteomes; UP000004416; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12178; 2-Hacid_dh_13; 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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 12..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 116..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 36735 MW; 1F6E99FECEBBFC46 CRC64;
MKQNVDSNRK KVFITGRIPS LAYEILSKEF DVTMHDDLRL LSKEEIIAGL KGKDALLCLL
SDAIDKDIIE ANPQLKVIAN YGAGYNNIDI AAAGEANIPV TNTPDVSTDA TADLTFGLIL
AIARRIVEGD KETRAGRFKG WAPLYHLGVD VTGKTLGIIG MGNIGKAIAR RAKGFDMKIV
YTSRTRLSEQ QEKELGFTYM SLEGVLKTAD FVSLSLSYSP ATHHMIGERE LETMKPSAYL
INTARGPLVD EKALLKALEN KSIAGAALDV YEFEPQITAG LEKLDQVILT PHIGNATVET
RDAMAEIAAG NIAAVLRGEA PLTCVNQNYL KKRNMAAK
//
