ID K9FRN3_PEND2 Unreviewed; 435 AA.
AC K9FRN3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=PDIG_48330 {ECO:0000313|EMBL:EKV11819.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV11819.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- FUNCTION: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can
CC use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC NAD(+). {ECO:0000256|ARBA:ARBA00037062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC EC=1.1.1.411; Evidence={ECO:0000256|ARBA:ARBA00036958};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00037979}.
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:EKV11819.1}.
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DR EMBL; AKCT01000196; EKV11819.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FRN3; -.
DR STRING; 1170229.K9FRN3; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_1_2_1; -.
DR InParanoid; K9FRN3; -.
DR OMA; QMFMQAS; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882}.
FT DOMAIN 6..161
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 173..293
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
SQ SEQUENCE 435 AA; 45860 MW; A8D89CEBDFD0475E CRC64;
MSTPAIGFVG LGAMGFGMAT HLVKEGYPVH GFDVFPASVE RFKTAGGIPA SSLRESAKGK
DFYVCMVASA PQVQSVLFGD GGIVGALPQN ATLLLCSTVP ASYAQSVAAE LVSVGRSDIA
FIDAPVSGGA LRAAAGTLSI MAGAPDAALE KGRFLLQEMS DVKKLYLVPG GIGAGSNMKM
VHQVLAGIHI LGAGEAQGFA ARLGLDAVKT SEAIKSSPAW TWMHENRLQR MLEEDWHPGA
SALTIILKDV GIITTSARQS QFPTPLCSTA EQVYLSALLQ GYGPVDDSSM VRQYFAEPIL
KVSSTQSEET AEALQLVLDL MEVTNLVAAA EAISFARYLK VDLKQFYTLV SDAAGASRQF
MTKGLEMIEG LGQGADGDSE TLDEATSRLE KAVQKARDLH CPLHLGNAAL SVLYMAKKYG
LGVERSASMV KAFET
//
