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Database: UniProt
Entry: A0A254QKT3_9RHOB
LinkDB: A0A254QKT3_9RHOB
Original site: A0A254QKT3_9RHOB 
ID   A0A254QKT3_9RHOB        Unreviewed;       388 AA.
AC   A0A254QKT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:OWU73070.1};
GN   ORFNames=ATO1_21190 {ECO:0000313|EMBL:OWU73070.1};
OS   Phaeobacter sp. 22II1-1F12B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU73070.1, ECO:0000313|Proteomes:UP000197279};
RN   [1] {ECO:0000313|EMBL:OWU73070.1, ECO:0000313|Proteomes:UP000197279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU73070.1,
RC   ECO:0000313|Proteomes:UP000197279};
RA   Lai Q., Li G., Shao Z.;
RT   "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL   Submitted (APR-2013) 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:OWU73070.1}.
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DR   EMBL; AQQP01000016; OWU73070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254QKT3; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000197279; 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:UP000197279}.
FT   DOMAIN          2..382
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         28
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         81..83
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         110
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         131
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         133
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         159
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         168
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         255
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         277
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         279
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         282
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   388 AA;  42883 MW;  DE0A1B2959FD6C8A CRC64;
     MDLHGKYPGL YDLKKRARRR IPKFVWEYLD SGTGQEATKQ RNRLALDRIG FEPSILHGEQ
     TPNLRQEFLG HEFPLPFGIS PVGMSGLIWP DAERLLAKAA AEAGLPYTLS TVASQSPEDV
     APVLGKHGWF QMYPPKDEAI RKDMLQRARD SGFTTLVLTA DVPVSSRRER QTRSGLTQPP
     RLTPRLMAQV MRCPSWAQGM ARLGMPHMRG LDKYIGEEHA NLPSTAHVGY LLRTSPDWEY
     ARWLRDHWDG PFVVKGVMRA YDARALEDLG VDAIWVSNHA GRQFDGAMAS IEALPAIRAA
     TGLPLIFDGG VEGGLDILRA LALGADFVML ARGFHYALGA LGSQGPAHLI DMLRLDLIAN
     MGQMGIETFS ALPKPISLDQ IDPAGRAY
//
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