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Database: UniProt
Entry: A0A9P4LNF1_9PLEO
LinkDB: A0A9P4LNF1_9PLEO
Original site: A0A9P4LNF1_9PLEO 
ID   A0A9P4LNF1_9PLEO        Unreviewed;       340 AA.
AC   A0A9P4LNF1;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 6.
DE   SubName: Full=Cytochrome b2 {ECO:0000313|EMBL:KAF2031983.1};
GN   ORFNames=EK21DRAFT_99303 {ECO:0000313|EMBL:KAF2031983.1};
OS   Setomelanomma holmii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Setomelanomma.
OX   NCBI_TaxID=210430 {ECO:0000313|EMBL:KAF2031983.1, ECO:0000313|Proteomes:UP000799777};
RN   [1] {ECO:0000313|EMBL:KAF2031983.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 110217 {ECO:0000313|EMBL:KAF2031983.1};
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:KAF2031983.1}.
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DR   EMBL; ML978176; KAF2031983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P4LNF1; -.
DR   OrthoDB; 1925334at2759; -.
DR   Proteomes; UP000799777; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase 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   PANTHER; PTHR10578:SF140; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000799777};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..340
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040118746"
FT   DOMAIN          61..339
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         126
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         159
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         168
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         208
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         230
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         232
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         235
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         266..270
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         289..290
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   340 AA;  37588 MW;  9A6AF95318BAFA06 CRC64;
     MKYTLFSHLF ATAILAARPF LNKPDTGIDD ALAIPQNGSL PDLSRLLGLP DFHWAARHVG
     EWSYRNNLEA FHRLRFRPRV MVDVVDIEAS LGILGFKFSA PFFISLSATA GMVHPKAERG
     LPSLASTLSM SDVAEARVTQ DQILFNRIEQ SGAKATVLTV DSAGDRTRHR ALRYVPDTNI
     ARTVRYTYMT WPYYQQLQNM TSLHIILKGI QTVEDARMAI KVGAPAIFLS NHGGRMLDGA
     PSTIEVALEI LKHDPIIFQQ TEVYADGGVR YDTDILKLLA LGVRAVGLGR PFMFANVFGA
     EGVARAIQLL KREVATSAAA LEVRNFKRID HTNVESTPNG
//
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