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).
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; 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
//