ID A0A1V6V5A3_9EURO Unreviewed; 955 AA.
AC A0A1V6V5A3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=PENCOP_c001G06061 {ECO:0000313|EMBL:OQE45864.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE45864.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000256|ARBA:ARBA00005715}.
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:OQE45864.1}.
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DR EMBL; MDDG01000001; OQE45864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6V5A3; -.
DR STRING; 36646.A0A1V6V5A3; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
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 InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_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; 2.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF142764; YgbK-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..167
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 174..293
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 319..431
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 485..722
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 749..945
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 955 AA; 103674 MW; 2CA39C185A8B0414 CRC64;
MAAKPKVAFI GLGAMGMGMA VQLLEDGFAV TGFDVNPMAL EKLLAMGGEA ADDPKTCVQD
ASFVICMVAN SMQTEDAFFA DSTGALFGLT QNAVVILCST VAPGFPVEIL GRIHHVFQRP
DVQVLDCPVS GGTIRAARGM LTILSSGPTG VLKTAQPILK SMSENLYEIE GGLGAANKVK
LINQHLAGVH IAVSAEAMGL AATLGVNTKE FYAAVLKGPA CSWMFENRVP HMLSNDWTPH
SAISIFVKDM RIVTSEGLLQ DFPLYIASAT ERLYQYAARM GYGKDDDASL VRIFLAQTPS
LVSEATHFQN SDNARASELI CQLLETVHTL AAVEALALGE KLGLSINTLT SIISNAAGAS
ESFKEVASMI LAGDLSSGYT ITRTRNKLKE VIILAQMHNY PLQLTATIFQ LLQQAVTYGL
GEEGQAALVK LWTTSSLLVE PLTITEYDPI SLSELHSKLP KLEHKSENLL CNIQDHLRAE
QNFKLVVLDD DPTGTQTCHD INVLTMWDVD LLASEFLTEG GGFFILTNSR SLPPDEARTL
VSEILRNVSR AAAMTGKQFE VVLRGDSTLR GHFLEEIESH IDTIGLPNVW ILAPFFGPGV
RYTIDDVQYV GDRDTLVPAA KTPFAKDRTF GYRSSNLREW VCEKAGSRFS SKDILSVTLE
DIRLGGISAV EQKLLRVPKG GILIVNAVQT EDMLMFSLAL LEVRKKHRLR FAYRTGASFV
SSRLGIPVKP VILPSQIPTF TPVRRTGGLV LAGSYVPKST KQIEALIQRS GGNLTALTVE
VQALLIELQR YPHIPTMLRH SPALLKIVVR ASEDLKNGKD VLVMTSRDLV TLDSVNSWAP
ETPKRITNLD INNLAANALV HIVRHLSVCP QYVLAKGGVT SSDAATAGIG IKRARVLGQA
APGVPVWWCQ SEEDLKCQDQ GGRDAKWNEV PLIIFPGNVG DEDSLADVVE QWALR
//
