ID A0A200HDF3_9ACTN Unreviewed; 387 AA.
AC A0A200HDF3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Lactate 2-monooxygenase {ECO:0000313|EMBL:OUZ10295.1};
GN ORFNames=BHE97_08065 {ECO:0000313|EMBL:OUZ10295.1};
OS Aeromicrobium sp. PE09-221.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1898043 {ECO:0000313|EMBL:OUZ10295.1, ECO:0000313|Proteomes:UP000195423};
RN [1] {ECO:0000313|EMBL:OUZ10295.1, ECO:0000313|Proteomes:UP000195423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE09-221 {ECO:0000313|EMBL:OUZ10295.1,
RC ECO:0000313|Proteomes:UP000195423};
RX PubMed=28218694;
RA Matobole R.M., van Zyl L.J., Parker-Nance S., Davies-Coleman M.T.,
RA Trindade M.;
RT "Antibacterial Activities of Bacteria Isolated from the Marine Sponges
RT Isodictya compressa and Higginsia bidentifera Collected from Algoa Bay,
RT South Africa.";
RL Mar. Drugs 15:E47-E47(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:OUZ10295.1}.
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DR EMBL; MIJB01000014; OUZ10295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200HDF3; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000195423; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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: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:OUZ10295.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000195423}.
FT DOMAIN 19..387
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 45
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 98..100
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 129
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 151
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 153
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 179
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 188
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 261
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 285
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
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 314..318
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 337..338
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 387 AA; 40599 MW; 3E065E97C03C7616 CRC64;
MSNFSDFQLG VYLEGILGQA PTMPFTFSEL EAQAQEAVVP DLWDYVAGGA GDEHTQQGNV
AAFERLGIRP RMLVGAGQRD QSVDLFGMSL PSPVFMAPIG VLGVLSSDGH GDIAAAKAAA
ATGVPLVGST LMQDPLEEVA ANLGQTPGMF QLYTPNDREL AVSLISRAES AGYRALVVTL
DTWTLGYRPR DLRHGTFPQL GGAGLANYTS DEVFLRRLPA ERRDDPAAAV EQWAGVFGNP
TLSWADLDWL RGSTSLPLIL KGICAAEDVR QARDAGVDGI YCSNHGGRQA ASAPALTFLP
EVVAAAGDLP VLFDSGVRSG VDIVKALALG ATAVGIGRPY GYGAALGATD GIVHVLKSLL
AEMDLTMALN GYASITELHP DILLPVP
//
