ID Q92TW9_RHIME Unreviewed; 301 AA.
AC Q92TW9;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=SM_b20668 {ECO:0000313|EMBL:CAC49775.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB {ECO:0000313|EMBL:CAC49775.1,
OG ECO:0000313|Proteomes:UP000001976}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC49775.1, ECO:0000313|Proteomes:UP000001976};
RN [1] {ECO:0000313|EMBL:CAC49775.1, ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|EMBL:CAC49775.1,
RC ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorholter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puhler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2] {ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591985; CAC49775.1; -; Genomic_DNA.
DR PIR; G96013; G96013.
DR RefSeq; NP_437915.1; NC_003078.1.
DR RefSeq; WP_010976192.1; NC_003078.1.
DR AlphaFoldDB; Q92TW9; -.
DR EnsemblBacteria; CAC49775; CAC49775; SM_b20668.
DR GeneID; 61601285; -.
DR KEGG; sme:SM_b20668; -.
DR PATRIC; fig|266834.11.peg.6296; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_2_5; -.
DR OrthoDB; 9812907at2; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:CAC49775.1};
KW Plasmid {ECO:0000313|EMBL:CAC49775.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001976}.
FT DOMAIN 4..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 167..287
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 301 AA; 30331 MW; B06223C0D4E64DDA CRC64;
MASKIAVLGL GSMGFGMACS MKSAGLDVLG YDVAPPAVER FVAEGGRGAG TPGEAVTGAD
IIVSIVVSGA QTEAVLFGPN GVAGAMKPGA AFISSATMDP AIARDLAQRL EALGLHYLDA
PISGGAAKAA KGELTIMASG SPQAFAAARP ALDAMAAKVY ELGGTAGTGA AFKMINQLLA
GVHIAAACEA IAFAAKQGLD LDKVYEVITA SAGNSWMFEN RIPHVLAGDY APLSAIEIFV
KDLGIVQDMA RAERYPVPLV AAALQMYLAA SGAGMGRDDD SSLARLYAQL SGATLPGTNN
P
//
