ID A0A9P4GXP5_9PLEO Unreviewed; 411 AA.
AC A0A9P4GXP5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Oxidase FUB9 {ECO:0000256|ARBA:ARBA00073420};
DE AltName: Full=Fusaric acid biosynthesis protein 9 {ECO:0000256|ARBA:ARBA00083297};
GN ORFNames=EK21DRAFT_81103 {ECO:0000313|EMBL:KAF2023377.1};
OS Setomelanomma holmii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Setomelanomma.
OX NCBI_TaxID=210430 {ECO:0000313|EMBL:KAF2023377.1, ECO:0000313|Proteomes:UP000799777};
RN [1] {ECO:0000313|EMBL:KAF2023377.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 110217 {ECO:0000313|EMBL:KAF2023377.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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:KAF2023377.1}.
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DR EMBL; ML978354; KAF2023377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P4GXP5; -.
DR OrthoDB; 1925334at2759; -.
DR Proteomes; UP000799777; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000056; hydroxyacid oxidase 2; 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 PANTHER; PTHR10578:SF149; 2-HYDROXYACID OXIDASE 2; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000799777}.
FT DOMAIN 6..404
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 193..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 32
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 85..87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 114
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 137
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 139
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 165
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 174
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 272
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 294
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 296
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 299
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 330..334
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 353..354
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 411 AA; 45250 MW; F2650166B78F1A67 CRC64;
MATSNAHDLD CLTIAELEKL AAERMDKQTR DYYNEGADHG STLAENMSAY QKYRIRPRVL
RDVSSVNTSV SIFDYTNSIP LGVAPTAMQG LAHPDGELAT ARACKNTGIV MGLSSFSTTS
LEDVKGALGP GHPAALQLYL FEEREESKRL IQRAKKAGYK AVFLTVDTPV LGRRNLEIRN
QFKLPKHLKV ANFNRDEDAH HSADSKEDKK KPDEETGANQ SRKRTQDSDS KRTPPKGPIT
FHTHAPNPTL VWERDIAWLK EICHPEMQVW VKGIATAEDA LLACHHGVDG IVVSNHGGRQ
LNGALATIDA LPEVVEAVRS QSKKIPVHVD GGIRHGTDVF KALALGADFV WVGRPVLWGL
AYKGQEGVEL CLKLLSDEVR LCMGLAGVTK VEDIGKEYLV KLDRSGFMSR L
//
