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Database: UniProt
Entry: A0A369VWA6_9SPHN
LinkDB: A0A369VWA6_9SPHN
Original site: A0A369VWA6_9SPHN 
ID   A0A369VWA6_9SPHN        Unreviewed;       377 AA.
AC   A0A369VWA6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-hydroxy-acid oxidizing protein {ECO:0000313|EMBL:RDE06119.1};
GN   ORFNames=DVW87_10395 {ECO:0000313|EMBL:RDE06119.1};
OS   Sphingomonas aracearum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2283317 {ECO:0000313|EMBL:RDE06119.1, ECO:0000313|Proteomes:UP000253918};
RN   [1] {ECO:0000313|EMBL:RDE06119.1, ECO:0000313|Proteomes:UP000253918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WZY 27 {ECO:0000313|EMBL:RDE06119.1,
RC   ECO:0000313|Proteomes:UP000253918};
RA   Zhiyong W., Qinglan Z., Zhiwei F., Ding X., Gejiao W., Shixue Z.;
RT   "a novel species of Sphingomonas isolated from the rhizosphere soil of
RT   Araceae plant.";
RL   Submitted (JUL-2018) 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:RDE06119.1}.
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DR   EMBL; QQNB01000002; RDE06119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369VWA6; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000253918; 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   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; 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:UP000253918}.
FT   DOMAIN          14..377
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         93..95
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         153
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         155
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         181
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         248
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         270
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         272
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
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         303..307
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   377 AA;  39138 MW;  A49CC76118544218 CRC64;
     MTSAGEAPLP PLATIPPDLR SLADYEQRAR AHLPAATWAH VEDRAGRGIT LDDNRAAFDR
     VRLLPRALAS LAGGSTASTL LGVHHPCPVL LGPVAYQRLA HAEGELATIR AATALGTGSV
     LSTLSSVPLE QVAAARLQAA DQLDVAPAPL WFQLYLQPRR EDSATLLRRA EAAGYQAIVL
     TIDAGVKRSG FVLPPGVEAA NLAGMEAPRH VASAGGRLLF GTALTDAVPT WEDLAWLRAA
     TDLPVLVKGM LVGDDLERAL AAGADGLILS NHGGRVLDGL PATLDLLPQV AAAVAGRVPV
     LLDGGVRTGT DVVKALCLGA IAVLVARPVL HALAVAGLAG VAHLCHLLRA ELELAMAQLG
     CATLDDLTEE RLFTTLR
//
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