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Database: UniProt
Entry: A0A1W0A2X9_9STRA
LinkDB: A0A1W0A2X9_9STRA
Original site: A0A1W0A2X9_9STRA 
ID   A0A1W0A2X9_9STRA        Unreviewed;       737 AA.
AC   A0A1W0A2X9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Peroxisomal (S)-2-hydroxy-acid oxidase {ECO:0000313|EMBL:OQS04634.1};
GN   ORFNames=THRCLA_20832 {ECO:0000313|EMBL:OQS04634.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS04634.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQS04634.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS04634.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
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:OQS04634.1}.
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DR   EMBL; JNBS01000582; OQS04634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W0A2X9; -.
DR   STRING; 74557.A0A1W0A2X9; -.
DR   OrthoDB; 276514at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 2.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 2.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 2.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT   DOMAIN          7..367
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   DOMAIN          370..730
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
SQ   SEQUENCE   737 AA;  80508 MW;  7885E41F604CB992 CRC64;
     MSPIVPGSDA TPLNVDEYEQ YARAYLPKST LDYYLSGADD MVTLKENRLA FQRLKLMPRV
     LRDVTHIDTS TTLLGHPVKT PVCIAPSAMQ RMAHPDGELA SSAAATAQGS CYILSTIGTT
     SIEDVAESSG SGLRWYQLYI FKDRELTRDL VVRAERAGYK ALVLTVDTPV LGSREPDIRN
     NFALPRHLKM ANFAHGKHAH RVNEVGLSQY TKELFDLNIT WGDVAWLKSI TSLPIVVKGV
     LTPEDAVIAC DVGCKGILVS NHGARQLDGV PATIEALPGI VQAVQGRAEV YLDGGVRRGT
     DVFKALALGA RAVFLGRPNL WGLAHNGQQG VEEVLKMLTS ELAHAMMFSA TTSLSEISPS
     YVRHEEYFLG SDATPLNLDE FEQYACAYLP KKTVDYYLSG ADDMVTLKEN RLAFQRLKLM
     PRILRDVTHI DTSTTLLGHP VKTPVCIAPS AMQKMAHPDG ESAASAAATA QGSCYILSTM
     STTSLEDVAV SSGDGLRWYQ LYVFKDRDLT RELVVRAERA GYKALVLTVD TPILGSREPD
     FRNNFALPSH LTMANFTHGK HAHGVNQMGL SKYTKELFDL NITWNDVAWL KSITSLPIVV
     KGVLTPEDAV KACEVGCKGI LVSNHGARQL DGVPATIEVL PAIVQAVQGR AEVYLDGGVR
     RGTDVFKALA LGARAVFLGR PNLWGLAHSG QQGVEDVLKM LTSELAHAMM FSATTSLKDI
     TPSYVRHEEY FRQPAKL
//
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