ID A0A2P4UDH8_9ACTN Unreviewed; 406 AA.
AC A0A2P4UDH8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Lactate 2-monooxygenase {ECO:0000313|EMBL:POM23110.1};
DE EC=1.13.12.4 {ECO:0000313|EMBL:POM23110.1};
GN ORFNames=BTM25_53160 {ECO:0000313|EMBL:POM23110.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM23110.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM23110.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM23110.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM23110.1}.
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DR EMBL; MTBP01000004; POM23110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UDH8; -.
DR Proteomes; UP000242367; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050040; F:lactate 2-monooxygenase activity; IEA:UniProtKB-EC.
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 Monooxygenase {ECO:0000313|EMBL:POM23110.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:POM23110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242367}.
FT DOMAIN 15..393
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 41
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 94..96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 123
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 182
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 286
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 288
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 291
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 319..323
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 342..343
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 406 AA; 42677 MW; F252C0F1043099E5 CRC64;
MAYTGSYQAQ VFADGGSPFP FTPKGLEEAA RRDLPRRYFD YIAGGAGRER TVAANEAAFG
RWGMTYRVLR DGAAADASTT VLGTPMSMPV MLAPAGVAEL AHPEAEVAAA RAAERAGAVQ
VLSAVTSASL EEVARAAPQG RRWFQFAWPD DEKLARSLIE RAEAAGYGAL VVMGDCHVAG
WRTRELSSGF FPFQHAHGLG NYISDRRFWE LAGFGSAPED RDRLTPEMIE AAASTWNRVF
TRPALLPADV ALLRSWTRLP IVVKGVCRPD EAARLCAAGV DALIVSNHGG RQLDGGVAAL
DCLPPVATAV AGRVPVLFDS GVRTGTDVLI ALALGADAVM IGRPWLYGLA VGGQAGVEHV
LRSLREEFTG ALALTGHRSC ASLSAADIVA VAPPTDPGTP GKGATS
//
