GenomeNet

Database: UniProt
Entry: A0A0A8F0G6_9ACTN
LinkDB: A0A0A8F0G6_9ACTN
Original site: A0A0A8F0G6_9ACTN 
ID   A0A0A8F0G6_9ACTN        Unreviewed;       399 AA.
AC   A0A0A8F0G6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Lactate 2-monooxygenase {ECO:0000313|EMBL:AJC61417.1};
GN   ORFNames=GZL_08894 {ECO:0000313|EMBL:AJC61417.1};
OS   Streptomyces sp. 769.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC61417.1, ECO:0000313|Proteomes:UP000031113};
RN   [1] {ECO:0000313|EMBL:AJC61417.1, ECO:0000313|Proteomes:UP000031113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=769 {ECO:0000313|EMBL:AJC61417.1,
RC   ECO:0000313|Proteomes:UP000031113};
RA   Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT   "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL   Submitted (DEC-2012) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003987; AJC61417.1; -; Genomic_DNA.
DR   RefSeq; WP_039639396.1; NZ_CP003987.1.
DR   AlphaFoldDB; A0A0A8F0G6; -.
DR   KEGG; stre:GZL_08894; -.
DR   HOGENOM; CLU_020639_0_1_11; -.
DR   Proteomes; UP000031113; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd03332; LMO_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   InterPro; IPR037350; LMO_FMN.
DR   PANTHER; PTHR10578:SF67; PEROXISOMAL (S)-2-HYDROXYACID OXIDASE GLO3-RELATED; 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   Monooxygenase {ECO:0000313|EMBL:AJC61417.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          23..392
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         49
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         102..104
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         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         190
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         263
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         285
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         287
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         290
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         318..322
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         341..342
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   399 AA;  42621 MW;  6FF5AC5D9A6263F9 CRC64;
     MAAPRRGFAD YQFEIYLKGL EDQVPPFTTD LSALEDAARD RIDPQPYGYV AGAAGTGATA
     RANRAGFDAH RIVPRMLRDA APRDLRTTVL GSELAAPVLL APIGVQSALH PDGELATARA
     AEATGIAMVL STASSHTIEE VAEANGTGQR WFQLYWPHDE EVTASILARA RATGYTTLVV
     TLDTWQLAWR PHDLDQAYLP FLRGNGVAIP LSDPVFRSRL DRPVEEDPRA AAMQWLPIFS
     GTAHTWDELG FLREHWDGPI VLKGILHPQD ARRAVSAGMD GVVVSNHGGR QVDGAVAALD
     ALVDVVAEVG GETEVLFDSG IRSGADAFKA LALGARAVLL GRPYVYGLAL GGTDGVRHVV
     RSLLADLDLT MGLVGCTRVA QIGPDTLHRP APAGGEARR
//
DBGET integrated database retrieval system