ID A0A2U1WLS8_9PROT Unreviewed; 312 AA.
AC A0A2U1WLS8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:PWC52468.1};
GN ORFNames=TSO221_14325 {ECO:0000313|EMBL:PWC52468.1};
OS Azospirillum sp. TSO22-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC52468.1, ECO:0000313|Proteomes:UP000245126};
RN [1] {ECO:0000313|EMBL:PWC52468.1, ECO:0000313|Proteomes:UP000245126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC52468.1,
RC ECO:0000313|Proteomes:UP000245126};
RA Jang J., Ishii S.;
RT "Comparative genome analysis of Azospirillum sp. strains.";
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|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:PWC52468.1}.
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DR EMBL; LGQZ01000053; PWC52468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1WLS8; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000245126; 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; cd12156; HPPR; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000245126}.
FT DOMAIN 7..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 32377 MW; A0463537E5151AC0 CRC64;
MKPEIILVEP MMASVEAALD AAYTVHRLAA APDRAALLAA VGPRVRAVVT GGATGVSNAV
MDACPNLGVV TINGVGTDAV DLRYAAGRGI RVTNTPGVLT EDVADLALGL IIAVSRRLIV
GDRFVRAGQW PKAKLPLARK VTGKRLGIFG LGRIGRAIAE RAAGFGMSIA YTNRTVCEDV
PYRCLGSLEE LARESDILVV AASAGPENRN LVGRAVLDAL GPEGVLINVA RGSIVDEAEL
VAALTEGRLG AAGLDVFADE PNVPQALWSL DNVVLQPHVA SATVETRTAM ADLVLANLEA
FFAGQPLPTP VV
//
