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
//