ID A0A077DD62_9BURK Unreviewed; 319 AA.
AC A0A077DD62;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dihydrofolate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=IX83_05105 {ECO:0000313|EMBL:AIL32770.1};
OS Basilea psittacipulmonis DSM 24701.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Basilea.
OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32770.1, ECO:0000313|Proteomes:UP000028945};
RN [1] {ECO:0000313|EMBL:AIL32770.1, ECO:0000313|Proteomes:UP000028945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32770.1,
RC ECO:0000313|Proteomes:UP000028945};
RX PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA Francois P., Pilo P., Frey J., Schrenzel J.;
RT "A genomic perspective on a new bacterial genus and species from the
RT Alcaligenaceae family, Basilea psittacipulmonis.";
RL BMC Genomics 15:169-169(2014).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP009238; AIL32770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077DD62; -.
DR STRING; 1072685.IX83_05105; -.
DR KEGG; bpsi:IX83_05105; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_4; -.
DR Proteomes; UP000028945; Chromosome.
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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000028945}.
FT DOMAIN 42..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34777 MW; CA507198536097EF CRC64;
MVSIGVVQMQ TILTLTNLHP YLEAELPKHF RVLGASNLEE RNRLIQERGA DITGVIGAYN
IPFDLKWLAH MPNLKVISSF GVGYDVYDLA CLKAKNIALS NTPSVLNDTV ADTAMALLLA
ASRGLIQADK WVREGVWQSG KVFPLMSDIH HKKVGIVGLG AIGQVIAKRL TGFDADIRYF
SRTAKNVPYL FEPNLKKLAQ WADVLIVITV GGPETKHLIN KEILECLGEN GVLINVARGS
VVDENVLIDV LEQGKLGAAG LDVFANEPNV PSRLINLPNV VLSPHVGSAT QECRLEMAKL
TLNNLIQFFE SGTLITPVV
//
