GenomeNet

Database: UniProt
Entry: I2QCQ5_9BRAD
LinkDB: I2QCQ5_9BRAD
Original site: I2QCQ5_9BRAD 
ID   I2QCQ5_9BRAD            Unreviewed;       305 AA.
AC   I2QCQ5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE            EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN   ORFNames=Bra1253DRAFT_02230 {ECO:0000313|EMBL:EIG57561.1};
OS   Bradyrhizobium sp. WSM1253.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG57561.1, ECO:0000313|Proteomes:UP000005125};
RN   [1] {ECO:0000313|EMBL:EIG57561.1, ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|EMBL:EIG57561.1,
RC   ECO:0000313|Proteomes:UP000005125};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX   PubMed=26629308;
RA   Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA   Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA   Ivanova N., Kyrpides N., Reeve W.;
RT   "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT   Ornithopus compressus from the Greek Island of Sifnos.";
RL   Stand. Genomic Sci. 10:113-113(2015).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH600073; EIG57561.1; -; Genomic_DNA.
DR   RefSeq; WP_007593728.1; NZ_JH600073.1.
DR   AlphaFoldDB; I2QCQ5; -.
DR   GeneID; 66479213; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_2_5; -.
DR   OrthoDB; 9812907at2; -.
DR   Proteomes; UP000005125; Unassembled WGS sequence.
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:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_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; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          10..166
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          173..293
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   305 AA;  31528 MW;  B90E6173D0C83F96 CRC64;
     MSASTSQNQR IAVIGLGSMG FGMATSLKRA GHVVTGCDVS ADAVARFVTE GGAGAKTPAE
     AAKGADIVVS VVVNAAQTET ILFGKDGVAE TMAKDSVFLS SATMDPDVAR RLAKQLEATG
     RHYLDAPISG GAQRAAQGEL TILASGSPAA FEKARPALDA MAAKLYELGD AAGQGAAFKM
     INQLLAGVHI AAASEAIAFA AKQGLDIRKV YEVITASAGN SWMFENRMPH VLDGDYTPRS
     AVEIFVKDLG IIQDMARSAR FPVPVSAAAL QMFLMTSAAG MGRDDDASVA RMYAQVTGVK
     LPGDK
//
DBGET integrated database retrieval system