ID A0A1G4AWC0_9PEZI Unreviewed; 1135 AA.
AC A0A1G4AWC0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=CORC01_11292 {ECO:0000313|EMBL:OHE93427.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE93427.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHE93427.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE93427.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OHE93427.1}.
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DR EMBL; MJBS01000120; OHE93427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4AWC0; -.
DR STRING; 1209926.A0A1G4AWC0; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000176998; 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 Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..171
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 178..297
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 330..487
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 500..619
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 689..927
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 956..1122
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1135 AA; 119102 MW; A7CD919A1612D6BC CRC64;
MVATDTEATR VGFIGLGAMG SGMACNLSKK PSYRVQGHDV YPPSVQKFVA QGGTSGESPR
EVAKTSDILV CMAVNAQQID DILFNDQTGA LQTLPANATI LLCSTVPPTY HEALAPRIAA
TGRQDVLVVD SPVSGGTKRA ADGTLSIFAS GAPAALRRAD RVLRDMSEKL YIIPGGPGAG
SKIKMVNQLL VGTHIAAASE AMGLAAKAGL NTREVYNIIT NAAGNSWAYE NRVPHMLDGD
WTPLSALNIF VKDMGIVVST ARALQFPVPL ASVAEQLYIS GAAHGYGADD DSGLVRVFLP
GTPNAVKEQA GQLNTQKKLT PSSTPLEISK IGMVGLGAMG QGMAGSLLRA GFAVHGYDVY
GPAIDKFAAN GGKASKASSP AEAAKDADIL VLMVQNAAQA DDVLFGSGKA AETLPDGAIV
ILSSTVPPSF VRELEAKLTK TGKGLSLIDA PVSGGVVRAA NGTLTIISSG DEAVLSKVNS
PLLAMTGTSS NLCHVQGGVG AASSVKLINQ LLAGVHIAAA AEAMAFAARL GLDTRRAFEI
LGSAAAWSWM FENRVPQMLD ADWTPHSALA IFVKDLGIVL DEAKRLTYFA PISSAAHNMY
LAGASHGWTK ESDAGVVRLW ELTGLSVSEN AGPKAEESSG SVANIAGNEA GQEEGLPAQK
TIESLPAEYS GDVISSIRKV VDNSEVPVLV VLDDDPTGTQ TCHNIDVLTV WDAATLNDEF
SLKPTGFFIL TNSRALPSAE AKQLIVEICR NVKTAAEKAG KAFEIVLRGD STLRGHLPQE
PEAAEEALGK FDAWVVTPFF YQGGRYTIND VHYVKEGDVL VPASQTPFAQ DATFGYKNSN
LRKYILEKCG HRFDESSFLS VTLEDIRVRG PAGVTKKLLS VAPCSNTVVI VNAAAESDMH
IFVAGLLEAE KQGRRYLYRT GAAFVSSRLG IKGIPPLTMA DLGVSIQAGT RQPGGLIVAG
SYVPKTTAQL KVLRDRRGDK LAVIELDVAG LIESAEAAGD VVTAAAAETA NKLAAGEDVL
VMTSRELIKG DNALSSLQIG SKVARALVQL VEQIDVRPRY LIAKGGITSS DAATKGLKMR
RARIMGQAAP GVPLWKCDEE TSRHRGVPYV VFPGNVGSDS TLAEVVESWS IENVA
//
