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Database: UniProt
Entry: A0A0J1GDC0_9FIRM
LinkDB: A0A0J1GDC0_9FIRM
Original site: A0A0J1GDC0_9FIRM 
ID   A0A0J1GDC0_9FIRM        Unreviewed;       299 AA.
AC   A0A0J1GDC0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHS_0752 {ECO:0000313|EMBL:KLU73348.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU73348.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU73348.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU73348.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU73348.1}.
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DR   EMBL; JNGB01000004; KLU73348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1GDC0; -.
DR   PATRIC; fig|1504536.3.peg.4717; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0046487; P:glyoxylate metabolic process; 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   InterPro; IPR006398; Tartro_sem_red.
DR   NCBIfam; TIGR01505; tartro_sem_red; 1.
DR   PANTHER; PTHR43060:SF3; 2-HYDROXY-3-OXOPROPIONATE REDUCTASE; 1.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 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   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT   DOMAIN          7..166
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          169..289
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   299 AA;  30992 MW;  22C62F1014713212 CRC64;
     MEVMKMKVGF IGLGIMGKPM VRNLLKAGYE VVAFDVMEAN VEEAAADGAV PAQSSKAVAQ
     QCKTIITMLP NSPHVKAAVM GENGVLEGAQ EGSILIDMSS IAPLASQEIS RACAGKGVKM
     IDAPVSGGEP KAIDGTMSIM VGGDKKVFDQ VYDLLMVMGG SAVHCGDIGA GNTTKLANQV
     IVALNIAAVS EAFMLSTKAG VDPVRVFDAI KGGLAGSTVM NAKIPMITAG NFNPGFKIDL
     HIKDLNNALE TGHGVGAPLP MTALAMEMLQ TLRADGCGQQ DHSAIAKYYE KITGVEIRG
//
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