ID A0A0E0PW17_ORYRU Unreviewed; 1385 AA.
AC A0A0E0PW17;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI06G10350.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI06G10350.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR STRING; 4529.A0A0E0PW17; -.
DR EnsemblPlants; ORUFI06G10350.1; ORUFI06G10350.1; ORUFI06G10350.
DR Gramene; ORUFI06G10350.1; ORUFI06G10350.1; ORUFI06G10350.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG4153; Eukaryota.
DR HOGENOM; CLU_002829_2_0_1; -.
DR OMA; CQHLCSL; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
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 NCBIfam; TIGR00167; cbbA; 1.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF01116; F_bP_aldolase; 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; SSF51569; Aldolase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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:UP000008022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..158
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 171..276
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 325..458
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 488..608
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 656..904
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 929..1095
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1385 AA; 148780 MW; D9030447004861F1 CRC64;
MASGKVVSFV GADELGVSLA ASFVRSGAIV RCFVAPGGDG SATALAELGG VRCASPAEAA
RDAELVIVLS DTDGVDELFF GPEGIVKGLC SGAVVLIRST MLPSHLEKLN QKLADEKKNA
LLDGYIFSGL SDELKQKIVV VASGRHDVTE RTGQFFSGLD TAVYFVEGEF GSSSKIKLVN
DLLESIHFIA SIEAMFLGVR AGIHPSIIYD IISNAAGSSR IFVEIVPKLL REDSLLIDYL
ESSKTNAGYV MDMAKAVIFP LPLVAVSYQQ LIHGCSSANG DALVSPLKVW EQSFGVNIID
AASQQIYDAS KLADQLVMAC KTAKTIGFIG LGAMGFGMAS HLLKSGFSVI AYDVYKPTLA
RFTDLGGLTK DSPEEVSKDV EILVIMVANE VQAENVLYGN AGAVSVMAAG TSIILSSTVS
PGFVIKLKER LEAECRDIKL VDAPVSGGVK RAAEGTLTTN MQKLVHDCSI FYVTALSEKL
YVIKGGCGAA SSVKMVNQLL AGVHIASAAE AMAFGARLNL RTRRLFEIIQ HARGYSWMFG
NRVPHMLDND YTPYSAVDIF VKDLGIVSHE SSNARIPLHV SSIAHQLFLS GSASGWGRFD
DAAVVKVYET LTGVKVEGRP PMLNKEDVLS SLPAEWPEDP MDDLVSSASH NSKKILVVLD
DDPTGTQTVH DIEVLTECAI SLTWKLNCRP VEALAEQFQK LPACFFILTN SRSMTAEKAT
LLVKDICRNL EAAAKSVPGV SYTVVLRGDS TLRGHFPEEA DAVVSVLGEM DAWIICPFFL
QGGRYTIDDI HYVADSDRLI PAGETEFAKD AAFGYKSSNL RQWVEEKTKG RISENQVSTI
SVNLLRKEGP NAVCQHLCSL KKGSACIVNA ASERDMSVFA AGMIQAELKG KRFLCRTAAS
FVSARIAIKP KPPIRPTDLG LKRALTGGLI VVGSYVPKTT KQVDELRSQC EQSLRIIEVS
VEMISMKSAE DRDHEISRVI ELGNAYIQSR KDTLVVTSRQ LITGKTPEES LEINYKVSSA
LVEIVRGIGS RPRYILAKGG ITSSDLATKA LEARRAKVMG QALAGVPLWQ LGPESRHPGV
PYIVFPGNVG DNSALAKVVQ NWACPSRSSA KELLLNAENG GYAIGAFNVY NLEGIDAVVS
AAEAEKSPAI LQVHPSALKQ GGVPLVSCCI AAAEHASVPI TVHYDHGTSK SDLLQALEMG
FDSIMVDGSH LPLGKNILYT RSISSLAHSK GMLVEAELGR LSGTEDGLTV EEYEARFTDV
AQALEFIDET GIDSLAVCIG NVHGKYPPSG PNLRFDLLED LRALTMKKGV SLVLHGASGL
PHELVKECIA LGVRKFNVNT EVRNSYLESL KRPEKDLIHV MASAKEAMKA VVAEKMRLFG
SSGKA
//
