ID A0A1G6JVD0_9RHOB Unreviewed; 286 AA.
AC A0A1G6JVD0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN04488239_101449 {ECO:0000313|EMBL:SDC22729.1};
OS Ruegeria marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=639004 {ECO:0000313|EMBL:SDC22729.1, ECO:0000313|Proteomes:UP000199628};
RN [1] {ECO:0000313|Proteomes:UP000199628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9108 {ECO:0000313|Proteomes:UP000199628};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMZV01000001; SDC22729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6JVD0; -.
DR STRING; 639004.SAMN04488239_101449; -.
DR Proteomes; UP000199628; 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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000199628}.
FT DOMAIN 1..148
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 154..274
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 160
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 286 AA; 29106 MW; D370FA8F6F11EF75 CRC64;
MGHGMAASAL RGGHRVWGHD INEEQAARFR SLGGEAGSLS DHAGELDAVA VVVLNAAQTE
TVLFGAAGMV PQLRAGAVVL SCATVPPDFA RAMEARCAGH GVHYLDAPIS GGSVKAAEGR
LSVMASGTQA AFSAARALLS SIAETVFELG DAAGAGSAMK AVNQMLAGVH IAAMAEALTF
GMTQGIAPDQ FLEVISKCAG TSWMLQNRAP HVVEGDYTPH SSVNIWPKDL GIVLDIARQA
EFAAPITAAA MQQFLAAAGM GLGSEDDAAV AKVYARNAGL TLPGEG
//
