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Database: UniProt
Entry: A0AAE3ENG7_9FLAO
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Original site: A0AAE3ENG7_9FLAO 
ID   A0AAE3ENG7_9FLAO        Unreviewed;       382 AA.
AC   A0AAE3ENG7;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   SubName: Full=Alpha-hydroxy-acid oxidizing protein {ECO:0000313|EMBL:MCF7568083.1};
GN   ORFNames=L3X37_06850 {ECO:0000313|EMBL:MCF7568083.1};
OS   Wocania arenilitoris.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Wocania.
OX   NCBI_TaxID=2044858 {ECO:0000313|EMBL:MCF7568083.1, ECO:0000313|Proteomes:UP001199795};
RN   [1] {ECO:0000313|EMBL:MCF7568083.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HMF6543 {ECO:0000313|EMBL:MCF7568083.1};
RA   Oh J.-S.;
RT   "Draft genome sequence of Sabulilitoribacter arenilitoris KCTC 52401.";
RL   Submitted (JAN-2022) 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:MCF7568083.1}.
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DR   EMBL; JAKKDU010000007; MCF7568083.1; -; Genomic_DNA.
DR   RefSeq; WP_237239432.1; NZ_JAKKDU010000007.1.
DR   AlphaFoldDB; A0AAE3ENG7; -.
DR   Proteomes; UP001199795; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
DR   GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
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; 2-HYDROXYACID OXIDASE 1; 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|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW   2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP001199795}.
FT   DOMAIN          4..382
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         30
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         83..85
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         112
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         133
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         135
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         170
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         257
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         279
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         281
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         284
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         312..316
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         335..336
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   382 AA;  42956 MW;  D066D5B5D8CE2F69 CRC64;
     MAIKFDTRYP SIEDLRRKAQ KKIPKFAFEY LDGGCNEDVN LIRNTAEIRD IQLKPNYLRK
     HHGSSLKTKL FGIEYDAPFG IAPVGLQGLM WPNSPEILAK AAFEHNIPFI LSTVTTTSIE
     RASELTEGKA WFQLYHPTEN RLRDDIIKRA EAAECPVLVI LCDVPTFGFR PRDIRNGLAM
     PPKMNLTNIL QAIGRPHWSL QTLKHGIPNF EVLKPYMPKD LDLKQLGKFM DQTFSGRLNE
     EKIKPIRDMW KGKLVLKGVA SEYDTEEAIR LGLDGIIVSN HGGRQLDAGQ STVKPLATIA
     EKYGDKITVM MDSGIRSGPD VARSMASGAK FTFMGRSFMY GVSALGKKGG NHTISLLKTE
     LQQVMEQLCC EKTTDFPYHL IK
//
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