ID A0A1F5L678_9EURO Unreviewed; 784 AA.
AC A0A1F5L678;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=PENARI_c026G07974 {ECO:0000313|EMBL:OGE48734.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE48734.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE48734.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE48734.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:OGE48734.1}.
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DR EMBL; LXJU01000026; OGE48734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5L678; -.
DR STRING; 1835702.A0A1F5L678; -.
DR OrthoDB; 879734at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd08252; AL_MDR; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF54; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..784
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519291"
FT DOMAIN 67..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 784 AA; 86725 MW; 9D0B70A0F4783CB2 CRC64;
MLLYRSLFAA FLLSLSAVAW QHETNLSTAN PLSAGCAKAC AELSSEFGPN LHYPADGNFT
VWDAKQTEVE SACRVEPSNS QDVSKVLSIL VDHWCRFAVK GGGHARNSDD SVSVGGVTID
MHLMKSIQVA PDQKTVNLGS GHVLYTMYHG LEAFNLTTIG GRVADVGLGG YALGGGISNL
SPKYGLAVDN IFEYEIVLPN ATIVHASEHH NSDLYFALRG GMNNFGIVTR YTMRAVPQKY
ILGGDKTYSS IQKDKIANEA FDLTTTWKND TDMAFSYGYS YDQASDQFSL SFSHAYARPV
LHPAPFTRLE RIPYKSSTVR IDRMSNLSLE GASHTPSGSR NLFATMTYQL SADMDRRIME
IMAEEIQPIK HVAHFFPNVI FQPLYEGAIR AGHERGGNAL GIKADGPLTI CLLTVMWTDR
QDDDAVNAFV QKWIRRVQAA TVQAGSHHHW LYINYAYHQQ DPFSGYGQRN KQRLIDVQKA
IDQRGVFTSR DYYTRVPRPY QICGYDGAGI VMKAGPDCTL FSEGDEVFYS GSPVRHGSNA
EFQLVDERSV GHKPKRLDMT EAASMPLTYI TAYQALVEQM EIETKENAAV LIINGAGGVG
AVASQIARQL LELPVVITTA SRPESVDFTK RMGATHVLNH RDDLAKQIQN LNLDVPVKYI
FITHSADQYM DACAKICMPF GKVCSIVQGQ AKMYGTEFMA KSLTFIWCLI GTKPVYHTDV
ESHHRILEDL SRLLDSGRIR CHLTSRFGLT LNGLREAHRS IESGGNIGKT GLTIGDIGDA
ERFM
//
