ID I1Q1C5_ORYGL Unreviewed; 1376 AA.
AC I1Q1C5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA06G0093800.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA06G0093800.1}
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; 4538.I1Q1C5; -.
DR EnsemblPlants; ORGLA06G0093800.1; ORGLA06G0093800.1; ORGLA06G0093800.
DR Gramene; ORGLA06G0093800.1; ORGLA06G0093800.1; ORGLA06G0093800.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG4153; Eukaryota.
DR HOGENOM; CLU_002829_2_0_1; -.
DR OMA; CQHLCSL; -.
DR Proteomes; UP000007306; 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 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..483
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 490..610
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 658..895
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 920..1086
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1376 AA; 147514 MW; 1C0F0D6044FE157B CRC64;
MASGKVVSFV GADELGVSLA ASFVRSGAIV RFFVAPGGDG 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 DSPEEVTKDV EILVIMVANE VQAENVLYGN AGAVSVMAAG TSIILSSTVS
PGFVIKLKER LEAECRDIKL VDAPVSGGVK RAAEGTLTII ASGTDEALQC TGSVLSALSE
KLYVIKGGCG AASSVKMVNQ LLAGVHIASA AEAMAFGARL NLRTRRLFEI IQHARGYSWM
FGNRVPHMLD NDYTPYSAVD IFVKDLGIVS HESSNARIPL HVSSIAHQLF LSGSASGWGR
FDDAAVVKVY ETLTGVKVEG RPPMLNKEDV LSSLPAEWPE DPMDDLVSSA SHNSKKILVV
LDDDPTGTQT VHDIEVLTEW PVEALAEQFQ KLPACFFILT NSRSMTAEKA TLLVKDICRN
LEAAAKSVPG VSYTVVLRGD STLRGHFPEE ADAVVSVLGE MDAWIICPFF LQGGRYTIDD
IHYVADSDRL IPAGETEFAK DAAFGYKSSN LRQWVEEKTK GRISENQVST ISVNLLRKEG
PNAVCQHLCS LKKGSACIVN AASERDMSVF AAGMIQAELK GKRFLCRTAA SFVSARIAIK
PKPPIRPTDL GLKRALTGGL IVVGSYVPKT TKQVDELRSQ CEQSLRIIEV SVEMISMKSA
EDRDHEISRV IELGNAYIQS RKDTLVVTSR QLITGKTPEE SLEINYKVSS ALVEIVRGIG
SRPRYILAKG GITSSDLATK ALEARRAKVM GQALAGVPLW QLGPESRHPG VPYIVFPGNV
GDNSALAKVV QNWACPSRSS AKELLLNAEN GGYAIGAFNV YNLEGIDAVV SAAEAEKSPA
ILQVHPSALK QGGVPLVSCC IAAAEHASVP ITVHYDHGTS KSDLLQALEM GFDSIMVDGS
HLPLGKNILY TRSISSLAHS KGMLVEAELG RLSGTEDGLT VEEYEARFTD VAQALEFIDE
TGIDTLAVCI GNVHGKYPPS GPNLRFDLLE DLRALTMKKG VSLVLHGASG LPHELVKECI
ALGVRKFNVN TEVRNSYLES LKRPEKDLIH VMASAKEAMK AVVAEKMRLF GSSGKA
//
