ID A0A0P6WZQ7_9CHLR Unreviewed; 327 AA.
AC A0A0P6WZQ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrofolate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC812_16000 {ECO:0000313|EMBL:KPL72336.1};
OS Bellilinea caldifistulae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Bellilinea.
OX NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL72336.1, ECO:0000313|Proteomes:UP000050514};
RN [1] {ECO:0000313|EMBL:KPL72336.1, ECO:0000313|Proteomes:UP000050514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL72336.1,
RC ECO:0000313|Proteomes:UP000050514};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL Submitted (JUL-2015) 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:KPL72336.1}.
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DR EMBL; LGHJ01000024; KPL72336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P6WZQ7; -.
DR STRING; 360411.AC812_16000; -.
DR PATRIC; fig|360411.5.peg.1073; -.
DR Proteomes; UP000050514; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050514}.
FT DOMAIN 34..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 327 AA; 36060 MW; 56E7F8786EF3E187 CRC64;
MMYTVLLSAP YMLPVVERFR PLFDHYGLTV IVPPVHERLS EQEILAYAGR FDATICGDDR
YTERVLQACA PRLKVISKWG TGIDSIDRAA AARLGIQVRN TPNAFTLPVS DSVLGYILAF
ARQLPWMDRA MKDGRWEKLP GRSLSECTLG VVGVGNVGKA VLRRARAFGM RLLGNDIVPI
APDFVLENGV EMTGLRDLLE RSDFISLNCD LNPTSYHLIN AETLGWVKPG AVLINTARGP
VVDEPALIAA LQEGRLAGAA LDVFEVEPLP LDSPLLKMDN VLLAAHNSNS SPAAWERVHW
NTIRNLLDGL GLDVSGLEEW RKRLGRD
//
