ID A0A1W6L9Z5_9BURK Unreviewed; 379 AA.
AC A0A1W6L9Z5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE SubName: Full=Alpha-hydroxy-acid oxidizing enzyme {ECO:0000313|EMBL:ARN21115.1};
GN Name=lldD {ECO:0000313|EMBL:ARN21115.1};
GN ORFNames=A4W93_15110 {ECO:0000313|EMBL:ARN21115.1};
OS Piscinibacter gummiphilus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN21115.1, ECO:0000313|Proteomes:UP000193427};
RN [1] {ECO:0000313|EMBL:ARN21115.1, ECO:0000313|Proteomes:UP000193427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS21 {ECO:0000313|EMBL:ARN21115.1,
RC ECO:0000313|Proteomes:UP000193427};
RA Tabata M., Kasai D., Fukuda M.;
RT "Complete genome sequence of natural rubber-degrading, novel Gram-negative
RT bacterium, Rhizobacter gummiphilus strain NS21.";
RL Submitted (APR-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}.
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DR EMBL; CP015118; ARN21115.1; -; Genomic_DNA.
DR RefSeq; WP_085751401.1; NZ_CP015118.1.
DR AlphaFoldDB; A0A1W6L9Z5; -.
DR STRING; 946333.A4W93_15110; -.
DR KEGG; rgu:A4W93_15110; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000193427; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
DR GO; GO:0006089; P:lactate metabolic process; IEA:InterPro.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000029; L-lactate dehydrogenase; 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; IPR020920; LldD.
DR NCBIfam; NF033901; L_lactate_LldD; 1.
DR NCBIfam; NF008398; PRK11197.1; 1.
DR PANTHER; PTHR10578:SF85; L-LACTATE DEHYDROGENASE; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW 2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000193427}.
FT DOMAIN 1..379
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 24
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 129
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 155
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 164
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 251
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 273
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 278
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 306..310
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 329..330
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 379 AA; 41398 MW; C8BCD6106ED83B14 CRC64;
MIISSSADYR TAAQKRLPPF LFHYLDGGAY AEQTLRRNVE DFAAVALRQR VLKDMSRLDT
SIELFGEKFS IPVALAPVGL GGMYARRGEV QSSQAADAHG IPFTMSSVSV CPIEEVAPKL
KRPMWFQLYV LKDRGFMKNA LERAQAAGCS TLVFTVDMPV PGARYRDAHS GMSGPNAPLR
RYWQAMMHPR WSLDVGLLGR PHDLGNISAY LGKPTGLADY MGWLGANFDP SISWRDLEWI
RDFWKGPMVI KGILDPDDAR DAVRFGADGI IVSNHGGRQL DGVLSSARAL PAIADAVKGQ
IKILADSGIR NGLDVVRALA LGADATMIGR AYIYALAVAG QAGVKHLLEL LEKEMRVAMT
LTSVAKVSDI NGDLLVRDR
//
