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Database: UniProt
Entry: A0A0F7JSR0_9GAMM
LinkDB: A0A0F7JSR0_9GAMM
Original site: A0A0F7JSR0_9GAMM 
ID   A0A0F7JSR0_9GAMM        Unreviewed;       290 AA.
AC   A0A0F7JSR0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Tartronate semialdehyde reductase {ECO:0000313|EMBL:AKH19491.1};
GN   ORFNames=AAY24_03025 {ECO:0000313|EMBL:AKH19491.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19491.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH19491.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19491.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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DR   EMBL; CP011412; AKH19491.1; -; Genomic_DNA.
DR   RefSeq; WP_046858429.1; NZ_CP011412.1.
DR   AlphaFoldDB; A0A0F7JSR0; -.
DR   KEGG; seds:AAY24_03025; -.
DR   PATRIC; fig|1543721.4.peg.634; -.
DR   OrthoDB; 9786703at2; -.
DR   Proteomes; UP000034410; Chromosome.
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; 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; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF15; 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.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT   DOMAIN          3..162
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          165..280
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   290 AA;  30566 MW;  2C3257909985A9C2 CRC64;
     MSKIGFIGVG IMGKPMAEHL QAGGHQLYLV RHRTPLPQAL LEAGAVECDS ARAVATQADI
     IIIMVPDTPH VERVLFGEDG VVAGLSPGKL LIDMSSISPI ETRTFATRIN ELGCDYLDAP
     VSGGEVGAKA ATLTIMVGGP ESAFEKARPL FDLMGKNITR VGENGAGQTC KVANQIVVAL
     TIEAVGEALL FASRAGVDPA RVREALMGGF AGSKILEVHG ERMIKRTFDP GFRIALHQKD
     LNLALTGARE LGLSLPNTAT TQELFNACNG DLDHSALVNA LEALADHRVA
//
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