ID A0A168HUF6_CORDF Unreviewed; 1074 AA.
AC A0A168HUF6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=LEL_05103 {ECO:0000313|EMBL:OAA78280.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78280.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78280.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78280.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA78280.1}.
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DR EMBL; AZHF01000003; OAA78280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HUF6; -.
DR STRING; 1081108.A0A168HUF6; -.
DR OrthoDB; 1121581at2759; -.
DR Proteomes; UP000076881; 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; 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; 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.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 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:UP000076881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 134..250
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 283..442
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 452..571
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 633..871
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 899..1065
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1074 AA; 113312 MW; 5D089039F26F713B CRC64;
MAGADTIGVI ASASTDCDWY IDALQKSGAT VHRYSTSAFS SHASSKADLH ALSCLPRKSA
IIVAEPVPDD FYESLGTTIA ERGRHDVQVI AASVSQKSIF VAGPNPAVDA YLALLQRPGI
PVHHVPGDFS SAAKLRLVHD HLLGVHTVAA AEAMGLAAKA GLNTNQVYDI IVNAAGSSTA
FETRAKKMLA GDWVPETPLF QTSDKLANAV AKTRDLRFPL PLASAAQQMC IMASSLGHGG
QDDSAVIRAY MPSDVDAIKQ ATRRSTTANE LTPTSSPGEI ASVGMVGLGA MGQGMAASLL
RAGFAVNGFD MNADAVDKFA SNNPKAQRAS SAADAMSASA VVILMVQNAA QADDILFGPD
NGADALSDHT VVILSSTVPP SFVRKLGARL QNLGRGISLL DAPVSGGVAR AANGTLAIMC
SGEDSSLAKS RSVLLSMTGP VTNLHTVQGG IGAASSVKLV NQLLAGVHIV AAAEAMAFAA
RLALHTRVAF DILIQTDAWS WMMENRTGQM LDADWTPHSA LAIFVKDLGI VLDEAKRLVF
YSPIASAAHT LYLNGAAHGW EKESDAGVVR LWELAGISVS GSASTQPKTT QTSNMNLPRL
AAAETLRSLP EEYSEDVLSS IRRVVDGGQV PTLVILDDDP TGTQTCHDIN VLAVWDAETL
AQEFSSGPAG FFILTNSRAL PSADARRLIV EICANVKAAA AKTNKTFEIV LRGDSTLRGH
LPEEPEAVEE ALGQFDGWVL TPFFSQGGRL TINDVHYVKE GDVLVPVSQT PFAQDATFGY
KNSNLRQYVL EKCGSRFDEE TFLSISIDDI RCGGPSAVAK RLLSVPSSPD LVIVVNAVVD
SDMHVFVAGL LEAEQHGRRY LFRTGAAFVS SRLAIKAIPP LRLEDLGVDK TARVQPGGLV
LAGSYVPKTT AQLQRLRERR GNKLHVLELP VAQLVSSVGA AGALVKEAAR GASETLAAGK
DVLVMTSREL VKGADALSSL SIGSRVAQAL VTLMEEINVR PRYIIAKGGI TSSDAATKGL
RMRRARVLGQ AAPGVPLWVC TEETSRHRAV PYVVFPGNVG SEDTLADIVE SWAI
//
