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Database: UniProt
Entry: X7E9U8_9GAMM
LinkDB: X7E9U8_9GAMM
Original site: X7E9U8_9GAMM 
ID   X7E9U8_9GAMM            Unreviewed;       378 AA.
AC   X7E9U8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=2-hydroxy-acid oxidase {ECO:0000313|EMBL:ETX12645.1};
GN   ORFNames=MUS1_03410 {ECO:0000313|EMBL:ETX12645.1};
OS   Marinomonas ushuaiensis DSM 15871.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX12645.1, ECO:0000313|Proteomes:UP000054058};
RN   [1] {ECO:0000313|EMBL:ETX12645.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX12645.1};
RA   Lai Q., Shao Z.S.;
RT   "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:ETX12645.1}.
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DR   EMBL; JAMB01000001; ETX12645.1; -; Genomic_DNA.
DR   RefSeq; WP_036158964.1; NZ_JAMB01000001.1.
DR   AlphaFoldDB; X7E9U8; -.
DR   STRING; 1122207.MUS1_03410; -.
DR   PATRIC; fig|1122207.3.peg.699; -.
DR   eggNOG; COG1304; Bacteria.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000054058; 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; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054058}.
FT   DOMAIN          1..378
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         23
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         76..78
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         105
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         126
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         128
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         163
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         251
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         273
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         275
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         278
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         306..310
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         329..330
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   378 AA;  42419 MW;  5B24DC09051E1396 CRC64;
     MILNTNDYRE KAKRFLPKFA FDYLDGGAEA ECTMMMNQKS FTNWGFIPSV LVDCDQCDTR
     VKWLDHTYSA PFAVAPTGYN GMLRHRADEH LAISADKSDI AYIQSTVSTS SLEDIGKLGI
     KKHWFQLYIL RDREITKDLL TRAKNQGCDT LVVSVDAVYF GNRERDKRHY SKPLKLSWKS
     HFNIAMHPEW LIKVILPQGM PTFGNLVPYL PSQYQKGVGA AAYFAKQMDP KLDWSTLSWL
     RDIWPGKLII KGVMSKSDAR KSIEYGCDGI VLSNHGGRQL DGTISPIEMI KSVREVIGQD
     PLLLVDSGFR RGTDIVKAIA LGANGVLIGR PLLYALAAEG QTGATKTINI LKKEVERTMA
     QLGCKTIYDI NSSMLKKL
//
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