ID A0A0S8AUF9_9BACT Unreviewed; 318 AA.
AC A0A0S8AUF9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Dihydrofolate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK71_01520 {ECO:0000313|EMBL:KPK02657.1};
OS Nitrospira bacterium SG8_35_4.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPK02657.1, ECO:0000313|Proteomes:UP000050997};
RN [1] {ECO:0000313|EMBL:KPK02657.1, ECO:0000313|Proteomes:UP000050997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPK02657.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK02657.1}.
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DR EMBL; LJTM01000016; KPK02657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AUF9; -.
DR PATRIC; fig|1704025.3.peg.1782; -.
DR Proteomes; UP000050997; 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; cd12172; PGDH_like_2; 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; 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; 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 17..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 35651 MW; B9A8D40EACCDCFB2 CRC64;
MKFKVLITAP YMQPVIQDYM HVFIENEIEI VAPLVRERLS EKELLGLISD IDGVIAGDDQ
FTSEVLRSAP KLKVLSKWGT GIDSFDQAAA QELGIAIRNT PGAFNEPVAD QVLGYMLSFA
RRIQWIDQRM KSGEWKKLTC FSLSNRTLGV IGVGNTGKAV IRRAKAFQMR LLGNDIAEMP
SEFIAETGIH MVDKETLLRE SDFVSLNCDL NPTSYHIMTR EEFSLMKPDA YFINAARGPL
VDEPAVIEAL QNKLIAGAAL DVFEDEPLPL ESPLRSMSNV LLSPHNANSS EEHWKRIHRS
TIANLLEELK KEEITVTH
//
