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Database: UniProt
Entry: T1YT96_9TRYP
LinkDB: T1YT96_9TRYP
Original site: T1YT96_9TRYP 
ID   T1YT96_9TRYP            Unreviewed;       293 AA.
AC   T1YT96;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:AGU67963.1};
DE            EC=1.1.1.169 {ECO:0000313|EMBL:AGU67963.1};
OS   Angomonas desouzai.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Angomonas.
OX   NCBI_TaxID=59800 {ECO:0000313|EMBL:AGU67963.1};
RN   [1] {ECO:0000313|EMBL:AGU67963.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TCC079E {ECO:0000313|EMBL:AGU67963.1};
RX   PubMed=24260300;
RA   Klein C.C., Alves J.M., Serrano M.G., Buck G.A., Vasconcelos A.T.,
RA   Sagot M.F., Teixeira M.M., Camargo E.P., Motta M.C.;
RT   "Biosynthesis of vitamins and cofactors in bacterium-harbouring
RT   trypanosomatids depends on the symbiotic association as revealed by genomic
RT   analyses.";
RL   PLoS ONE 8:E79786-E79786(2013).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KF160119; AGU67963.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1YT96; -.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 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   Oxidoreductase {ECO:0000313|EMBL:AGU67963.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..293
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004586430"
FT   DOMAIN          5..147
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          176..282
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   293 AA;  32237 MW;  95745250AD610CB3 CRC64;
     MKTVGLIGLG ALGIMFGWQL QQKLGNDFCV IVDEERKETY LRQGIFANGE PCQFRFVTPQ
     QASEPLDLLI FGTKIGGLRA AIATAKPFVG PTTVVLSLLN GVSSEEIIGE SYGAEKVLLA
     VSQEMDAVRV GTGVRYTNMG CIVYGEPNGE LTARVTEVER ILQKGGVVGR PSREAKRILW
     NKLMINVGVN QVSAAYNATY GDICKKPEVH EVFLGAMREA MMIGCKEGVD LSEDDVARWI
     SLVEKLDPNS FPSMLQDVRA KRYTEVELFG KTIVQLGKKS EFPPRSIRCL SRK
//
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