ID A0A0N1GGN2_9ACTN Unreviewed; 421 AA.
AC A0A0N1GGN2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Hem/flavin dehydrogenase {ECO:0000313|EMBL:KPI18890.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:KPI18890.1};
GN ORFNames=OK074_1354 {ECO:0000313|EMBL:KPI18890.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI18890.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI18890.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI18890.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI18890.1}.
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DR EMBL; LJCV01000055; KPI18890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GGN2; -.
DR PATRIC; fig|1592327.3.peg.1562; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; IPR023989; MftD.
DR NCBIfam; TIGR03966; actino_HemFlav; 1.
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; 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 ECO:0000313|EMBL:KPI18890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 2..384
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 392..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 81..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 109
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 131
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 157
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 166
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 255
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 277
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 310..314
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 333..334
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 421 AA; 44131 MW; 7FF843BF96BEF79E CRC64;
MGRNPWFETV AEAQRRAKKR LPSTVYGALL AGSERGRTID ANTAAFAELG FAPRVVGHHA
QRDLSTTVLG VPTSLPVLVS PTGVQAVHPE GEVAVARAAA GRGVLMGLSS FASKPVEEVA
AANPNFFYQL YWSGTREQMV QRMERARAAG AKALIVTLDW SFSHGRDWGS PSIPDKLDLR
TMLRFAPNVL PHPGWLWRFA RSGRVPDLTV PNLQPPGGQA PTFFGAYGEW MQTTPPTWDD
VAWLRAEWGG PFLLKGVTRV DDAKRAVDAG VAALSVSNHG GNNLDTTPAT IRILASVAEA
VGDQIEVLLD GGVRRGGDVA KALALGARAV LIGRAYLWGL AANGQAGVEN VLDILRGGLD
SAVLGLGHAS VHELSPDDLV IPPGFRLTLG GGADAGTDVD PDAGAADGSG PVPAAAHSRA
G
//
