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Database: UniProt
Entry: A0A1V2H3P2_9PROT
LinkDB: A0A1V2H3P2_9PROT
Original site: A0A1V2H3P2_9PROT 
ID   A0A1V2H3P2_9PROT        Unreviewed;       391 AA.
AC   A0A1V2H3P2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alpha-hydroxy-acid oxidizing enzyme {ECO:0000313|EMBL:ONG55501.1};
GN   Name=lldD {ECO:0000313|EMBL:ONG55501.1};
GN   ORFNames=BKE38_09180 {ECO:0000313|EMBL:ONG55501.1};
OS   Pseudoroseomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG55501.1, ECO:0000313|Proteomes:UP000188879};
RN   [1] {ECO:0000313|EMBL:ONG55501.1, ECO:0000313|Proteomes:UP000188879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3 {ECO:0000313|EMBL:ONG55501.1,
RC   ECO:0000313|Proteomes:UP000188879};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Roseomonas sp. strain M3.";
RL   Submitted (OCT-2016) 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:ONG55501.1}.
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DR   EMBL; MLCO01000073; ONG55501.1; -; Genomic_DNA.
DR   RefSeq; WP_076957057.1; NZ_MLCO01000073.1.
DR   AlphaFoldDB; A0A1V2H3P2; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000188879; 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:UP000188879}.
FT   DOMAIN          1..381
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        276
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         25
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         78..80
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         107
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         130
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         156
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         165
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         252
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         274
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         276
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
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         307..311
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   391 AA;  42318 MW;  7B674F7F1DE58651 CRC64;
     MPIATNIEDL RDIARRRIPR AIFDYADRGS YDEATLRANR EDLAALKLRQ RVMVDVSERS
     TATTMLGEKV TMPVAIAPTG LTGLFHADGE IHGCRAAHEF GIPFTLSTMS ICSIEDVAEA
     VQKPFWFQLY VMRDRGFSKS LVERAIAAKC SALVLTLDLQ IQGQRHRDIK NGLAVPPKLT
     LRNALDIATK PRWAMEVLRG KRKTFGNLTN APTGGSGLTT LSHWIAGQFD PSLSWKDVAW
     IRSIWPGKLI LKGVCDVDDA RIAAETGADA IVVSNHGGRQ LDGAPSSISL LPSVAEAVGD
     RTEVLFDGGV RSGQDVMKAM ALGAKGCMIG KAWLYGLAAG GHAGVTQMLE IIRKELDVSM
     ALTGIRDVRE ISPDVLHAPR HGDVVLPPGG R
//
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