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Database: UniProt
Entry: B7FWQ5_PHATC
LinkDB: B7FWQ5_PHATC
Original site: B7FWQ5_PHATC 
ID   B7FWQ5_PHATC            Unreviewed;       387 AA.
AC   B7FWQ5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEC49243.1};
GN   ORFNames=PHATRDRAFT_34800 {ECO:0000313|EMBL:EEC49243.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC49243.1, ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC49243.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC49243.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA   Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CM000609; EEC49243.1; -; Genomic_DNA.
DR   RefSeq; XP_002179420.1; XM_002179384.1.
DR   AlphaFoldDB; B7FWQ5; -.
DR   STRING; 556484.B7FWQ5; -.
DR   PaxDb; 2850-Phatr34800; -.
DR   GeneID; 7200351; -.
DR   KEGG; pti:PHATRDRAFT_34800; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   InParanoid; B7FWQ5; -.
DR   OrthoDB; 2670761at2759; -.
DR   Proteomes; UP000000759; Chromosome 6.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF25; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000759}.
FT   DOMAIN          85..377
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          194..350
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   387 AA;  42768 MW;  35E2BA208A05BD98 CRC64;
     MYRYFHFCST PGPITIEIRE SQGRRRFIEA NTASNGTSST MATRVFWRFH ARLTRPCRVV
     YAGPHFQAGL SYTQALVRER GLEQCVELVH APTDAQLWEL APTVDVAVPF MQSFRADFIE
     RASRMRLIMQ YGVGLEGVDV DSATKHGIAV SNIPAAGTGN AEATAEHAIF LSLSLLRRAF
     QDLPQRFQGR ILGGLPIPKS LFQKNVTVVG YGAVGSKICE YLNAMGAKVT VVRKHWTVEP
     ERGIHKARSL GECLPTTDLL ILACPLTTET FHMLNEETLS LLPRQGSLVV NIGRGPRVEH
     SAVWRALNSG RVGGYASDVG VGHPVKPSEP WDPDDDLSRH ANVLFTPHVG GYTYYSYNLM
     CKAVVDAIDD VRCGRPPDMG KFQVEVD
//
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