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Database: UniProt
Entry: A0A0A2L2A8_PENIT
LinkDB: A0A0A2L2A8_PENIT
Original site: A0A0A2L2A8_PENIT 
ID   A0A0A2L2A8_PENIT        Unreviewed;       319 AA.
AC   A0A0A2L2A8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Riboflavin synthase-like beta-barrel {ECO:0000313|EMBL:KGO73348.1};
GN   ORFNames=PITC_086360 {ECO:0000313|EMBL:KGO73348.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73348.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO73348.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73348.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO73348.1}.
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DR   EMBL; JQGA01000828; KGO73348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L2A8; -.
DR   STRING; 40296.A0A0A2L2A8; -.
DR   HOGENOM; CLU_003827_7_1_1; -.
DR   OMA; FHLYITN; -.
DR   OrthoDB; 3060848at2759; -.
DR   PhylomeDB; A0A0A2L2A8; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00322; FNR_like; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR46505; OXIDOREDUCTASE NAD-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46505:SF1; OXIDOREDUCTASE NAD-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          22..166
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  35408 MW;  8F160041F402C30A CRC64;
     MTSQRDDSVP HELRTAAEPR QNRLHPVRLS HIEQVNPSVR LLQFALPQEN NDTNQQPFSF
     LPGQWLDVHI PSISQAGGFT ITSTPADAQV LPPPEASIDS LACEALEPSS ESQGRPPYVE
     LAVQDSPGNP SAAWLWKPNE EILGKELNIR VGGSFVWPPT GVNINDVKNV VFVAGGVGIN
     PLISMLSHLN NNEPHTPNPT SIHILYSSRL PQDRETASAD AVLDQILFLP RLRQIVRSQE
     SSHRLRISLD LFLTNLASSP NLRSFRSPSD MNVHRWRISD RDLRSATVGT DGELDPRGTK
     LVEILGDGGA QRVFFEKWW
//
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