ID Q9LM23_ARATH Unreviewed; 1486 AA.
AC Q9LM23;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AAF78379.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2] {ECO:0000313|EMBL:AAF78379.1}
RP NUCLEOTIDE SEQUENCE.
RA Shinn P., Brooks S., Buehler E., Chao Q., Johnson-Hopson C., Khan S.,
RA Kim C., Altafi H., Bei Q., Chin C., Chiou J., Choi E., Conn L., Conway A.,
RA Gonzales A., Hansen N., Howing B., Koo T., Lam B., Lee J., Lenz C., Li J.,
RA Liu A., Liu K., Liu S., Mukharsky N., Nguyen M., Palm C., Pham P.,
RA Sakano H., Schwartz J., Southwick A., Thaveri A., Toriumi M., Vaysberg M.,
RA Yu G., Federspiel N.A., Theologis A., Ecker J.R.;
RT "Genomic sequence for Arabidopsis thaliana BAC T10O22 from chromosome I.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAF78379.1}
RP NUCLEOTIDE SEQUENCE.
RA Shinn P., Brooks S., Buehler E., Chao Q., Cheuk R., Johnson-Hopson C.,
RA Khan S., Kim C., Altafi H., Bei B., Chin C., Chiou J., Choi E., Conn L.,
RA Conway A., Gonzalez A., Hansen N., Howing B., Koo T., Lam B., Lee J.,
RA Lenz C., Li J., Liu A., Liu J., Liu S., Mukharsky N., Nguyen M., Palm C.,
RA Pham P., Sakano H., Schwartz J., Southwick A., Thaveri A., Toriumi M.,
RA Vaysberg M., Yu G., Davis R., Federspiel N., Theologis A., Ecker J.;
RL Submitted (JUN-2000) 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}.
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DR EMBL; AC069551; AAF78379.1; -; Genomic_DNA.
DR ExpressionAtlas; Q9LM23; baseline and differential.
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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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; 2.
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 5..86
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 193..310
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 347..514
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 521..641
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 688..975
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 1059..1196
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
SQ SEQUENCE 1486 AA; 160221 MW; 48B795C7DFDD396B CRC64;
MSGVVGFVGL DSFSFELASS LLRSGFKVQA FEISTELVEK FIELGGHKCD SPADVGKAAA
AVVVVLSHPD QIQDVIFGDE GVMKELLCRR LYASFLRRST EGRCIAFVFD NIDFATPETR
ETTYRFQFDT LSLRHEKREQ IFVVDAYVLK GMSELLDGKL MIIASGRSDS ITRAQPYLTA
MCQNLYTFEG EIGAGSKVKM VNELLEGIHL VAAVEAISLG SQAGVHPWIL YDIISNAAGN
SWIYKNHIPL LLKDDIEGRF LDVLSQNLAI VEDKAKSLPF PVPLLAVARQ QLISGISQMQ
GDDTATSLAK ISEKVLGVGI LEAANRELYK PEDLAKEITT QAKPVNRIGF IGLGAMGFGM
AAHLLKSNFS VCGYDISLRL AVSSVYKPTL VRFENAGGLA ANSPAEVTKD VDVLVIMVTN
EVQAEDVLYG HLGAVEAIPS GATVVLASTV SPAFVSQLER RLENEGKDLK LVDAPVSGGV
KRAAMGELTI MASGTDEALK SAGLVLSALS EKLYVIKGGC GAGSGVKMVN QLLAGVHIAS
AAEAMAFGAR LGLNTRKLFN VISNSGGTSW MFENRVPHML DNDYTPYSAL DIFVKDLGIV
TREGSSRKVP LHISTVAHQL FLAGSAAGWG RIDDAGVVKV YETLAGIKVE GRLPVLKKQD
LLKSLPAEWP SDPTTDIHRL NMGNSKTLVV LDDDPTGTQT VHDVEVLTEW SVESISEQFR
KKPACFFILT NSRSLSPEKA SELIKDICSN LCAASKEVGN ADYTIVLRGD STLRGHFPQA
SLEADAAVSI LGEMDAWIIC PFFLQGGRYT IDDVHYVADS DRLVPAGETE FAKDASFGYK
SSNLREWVEE KTAGVIPANS VQSISIQLLR KGGPDAVCEF LCSLKKVNFS KQISRRLLDV
AFRELLVFIV VESVSPSCVE SLNSISISYV NQGSTCIVNA ASERDMAVFA AGMIQAELKG
RSFLCRTAAS FVSALIGIIP KDPVLPKDFE SNKESSGALI VVGSYVPKTT KQVEELQSQH
NQNLRSIEVR EVDVTRDTYI SIYHMLCMLC LLSSSNDQQI SVEKVALKSS EVRDEEIRRA
VEMADAFLRA GRETLIMSSR ELITGKTSSE SLDINSKVSS ALVEVVSQIS TRPRYILAKG
GITSSDTATK ALKARRALVI GQALAGVPVW KLGPESRHPG VPYIVFPGNV GNSTALAEVV
KSWSVVAGRS TKELLLNAEK GGYAVGAFNV YNLEGIEAVV AAAEEENSPA ILQVHPGAFK
QGGIPLVSCC ISAAEQARVP ISVHFDHGTT KHELLEALEL GLDSVMVDGS HLSFTENLSY
TKSITELARS KNIMVEAELG RLSGTEDGLT VEDYEAKLTN VNQAQEFMET GIDALAVCIG
NVHGKYPKSG PNLKLDLLKE LHALSSKKGV FLVLHGASGL SENLIKECIE NGVRKFNVNT
EVRTAYMEAL SSGKKTDIVD VMSATKAAMK AVIADKIRLF GSAGKA
//
