ID A0A8J4E2X0_9ACTN Unreviewed; 355 AA.
AC A0A8J4E2X0;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Alpha-hydroxy-acid oxidizing enzyme {ECO:0000313|EMBL:GIJ60280.1};
GN ORFNames=Vau01_077960 {ECO:0000313|EMBL:GIJ60280.1};
OS Virgisporangium aurantiacum.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Virgisporangium.
OX NCBI_TaxID=175570 {ECO:0000313|EMBL:GIJ60280.1, ECO:0000313|Proteomes:UP000612585};
RN [1] {ECO:0000313|EMBL:GIJ60280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 16421 {ECO:0000313|EMBL:GIJ60280.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Virgisporangium aurantiacum NBRC 16421.";
RL Submitted (JAN-2021) 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:GIJ60280.1}.
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DR EMBL; BOPG01000051; GIJ60280.1; -; Genomic_DNA.
DR RefSeq; WP_204004343.1; NZ_BOPG01000051.1.
DR AlphaFoldDB; A0A8J4E2X0; -.
DR Proteomes; UP000612585; 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; 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:UP000612585}.
FT DOMAIN 1..354
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 129
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 157
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 166
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 225
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 249
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 252
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 280..284
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 303..304
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 355 AA; 37268 MW; E162C24CB914339C CRC64;
MDTPATLDEI REAALARLPV PARDFLEGGA GAETTLRRNR RAFQRWAFVP RVMNGLPAPT
TATRFLGVDL ALPVLTAPFG ADGLFHPDGQ IAVARANAAA GTASIVPEAG THPLEKVATA
VPGSAAFGQI HPLGTDDGFL DMVRRYEDAG YRGLCVTCDV PIGGWRERNL RNRYLPDYAL
FGGNYATIEQ ALGQLGQLLA PEAPVWSWHK LATLLARSAL PWIAKGIMTV DDAHAAVGAG
ASALLVSNHG GRQLDDQRAS LDALPEIRAA VGPDVPIALD SGVRRGTDVV KAIALGADVV
VIGRLAAYGL AAGGEDGVVR VLELLRTEIS TTLTLLGCGG LTDLNRDALV RVDAD
//
