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Database: UniProt
Entry: W4HGY5_9RHOB
LinkDB: W4HGY5_9RHOB
Original site: W4HGY5_9RHOB 
ID   W4HGY5_9RHOB            Unreviewed;       379 AA.
AC   W4HGY5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=FMN-dependent alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:ETW11391.1};
GN   ORFNames=ATO8_17010 {ECO:0000313|EMBL:ETW11391.1};
OS   Roseivivax marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW11391.1, ECO:0000313|Proteomes:UP000019063};
RN   [1] {ECO:0000313|EMBL:ETW11391.1, ECO:0000313|Proteomes:UP000019063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s10s {ECO:0000313|EMBL:ETW11391.1,
RC   ECO:0000313|Proteomes:UP000019063};
RX   PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA   Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT   "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT   Atlantic Ocean.";
RL   Antonie Van Leeuwenhoek 105:863-869(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:ETW11391.1}.
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DR   EMBL; AQQW01000012; ETW11391.1; -; Genomic_DNA.
DR   RefSeq; WP_043846264.1; NZ_AQQW01000012.1.
DR   AlphaFoldDB; W4HGY5; -.
DR   STRING; 1379903.ATO8_17010; -.
DR   PATRIC; fig|1317118.6.peg.3502; -.
DR   eggNOG; COG1304; Bacteria.
DR   Proteomes; UP000019063; 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:UP000019063}.
FT   DOMAIN          1..379
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         26
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         80..82
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         130
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         132
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         158
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         167
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         254
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         276
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
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         281
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         309..313
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         332..333
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   379 AA;  40113 MW;  338E1C6507C9FC73 CRC64;
     MARPLISSTD LRERAKARLP RFAFDYIDGG AGEEDALARS RRAYRETCLR PRVLVNSAEP
     ANLSHRFLNR DWALPFGIAP LGLPGLAWPG ADLAMARAAE AAGAPFVTAT PGTATLETVR
     AAAPTRSAFQ LYVGAATEIT DDLVARAERA GYDTLIVTAD VPRAGKRLRD LRNGFGLPLR
     ITPRLAMDLA LHPRWSLATW RAGAPHLINF AAYADDGAGA QTLAQLMARQ SSGRLDWAVL
     ARIRDRWSGA LVLKGVLDPE DAARAVGAGV DAIQVSNHGG RQLDGAPATL DALRAIREAL
     PADVPLAVDG GVRSGEDILK ALEAGADFVF LGRPFLYAVA AEGAAGPAAL FDMLAAELEA
     AMAQTGRRSI AGIRRCATD
//
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