ID A0A3M9Y7I5_9PEZI Unreviewed; 1132 AA.
AC A0A3M9Y7I5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=D7B24_007290 {ECO:0000313|EMBL:RNJ56453.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ56453.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ56453.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ56453.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RNJ56453.1}.
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DR EMBL; RBVV01000057; RNJ56453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9Y7I5; -.
DR STRING; 1051616.A0A3M9Y7I5; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000267145; 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; 2.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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; 2.
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; 2.
DR SUPFAM; SSF142764; YgbK-like; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..174
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 181..300
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 335..492
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 505..624
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 688..926
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 957..1123
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1132 AA; 119487 MW; 043FB493AF4B7486 CRC64;
MAQQSGTSLM STSVGFVGLG AMGFGMACNL QKGGKYIVKG YDVWQPSVER FVADGGHPGQ
SPRDVAHDSA FLVCMAANAQ QVDSILFDAA TGALEALPHN ATILLCSTVP PAYYDTLASQ
IAQLGRSDIL VVDCPVSGGT VRAANGTLTI FASGSSEALT RADQILHEMS EKLYGISGGP
GAASKVKMVN QCLVGTHIAA AAEAMGLAEK AGLDTREVFE IIKNAAGNSW AFENRVPHML
DADWTPRSAL DIFVKDMGIV VSSARSLQFP LPLASAAEQL YIWGSAQGYG REDDSGLVRV
FQQNSPVATK DSDSAAPAAA LANPTPVTTP LEISKVGMIG LGAMGQGMAS SMIRGGFAVH
GYDVYEPAIQ KFVSGGGKAS AATSPADAAR GAEVLVLMVQ NATQATDALF GSGDAAAALP
DDAIVILSST VPPSFVRSLE KRLAGLGRGI TLLDAPVSGG VVRAANGNLT IICSGEESTI
SKANGVLLSM TGLATNLCQV KGGVGAASSV KLINQLLAGV HIAAAAEAMA FAARLGLDTR
QIFELLKNAA AWSWMFENRV PQMLEADWTP HSALAIFVKD LGIVLDETKR LMYFAPMSSA
AHTLYLAGAA KGWSKEADAG VVRWWEGAGV SVSGSAGRPE PHTTNEAVQA AAQPLPAKET
IEALPAEFPH DVLESTKKYV DGGEAPVLVV LDDDPTGTQT CHDIDVLMVW DVETLQSQFE
RESRGFFILT NSRALPGPEA RNLILEICEN VKEAAQRTNK RFDVVLRGDS TLRGHLPEEP
EAVEQAMGKF DAWVLTPFFL QGGRYTLDDV HYVKEGDVLV PASQTPFAQD ATFGYQNSNL
RQYILEKCGS RFNESSFLSI TIDDIRVGGP QGVKAKLLSR PAGSDGVVIV NAAAESDMDV
FVSGLLAAEK EGRRYLYRTA AAFVSSRLGI KGIPPLRMAD VQPPTTSGSA SSHAGGLILA
GSYVPKTTAQ LKVLRERRQD KLAVVELEVA DLIKSAESER AIVDKAAAEA NDQISAGKDI
LVMTSRTLVK TSDAISSLEI GSKVASALVR LLEQIRVRPR YVIAKGGITS SDAATKGLKM
RRARIMGQAA PGVPLWRCDE ETSRHRGVPY VVFPGNVGSE STLAEIVESW AA
//
