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Database: UniProt
Entry: E1Z3H1_CHLVA
LinkDB: E1Z3H1_CHLVA
Original site: E1Z3H1_CHLVA 
ID   E1Z3H1_CHLVA            Unreviewed;       476 AA.
AC   E1Z3H1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CHLNCDRAFT_133629 {ECO:0000313|EMBL:EFN59850.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN59850.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN59850.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; GL433835; EFN59850.1; -; Genomic_DNA.
DR   RefSeq; XP_005851952.1; XM_005851890.1.
DR   AlphaFoldDB; E1Z3H1; -.
DR   STRING; 554065.E1Z3H1; -.
DR   GeneID; 17359157; -.
DR   KEGG; cvr:CHLNCDRAFT_133629; -.
DR   eggNOG; ENOG502QVGN; Eukaryota.
DR   InParanoid; E1Z3H1; -.
DR   OMA; HHEFRTM; -.
DR   OrthoDB; 455805at2759; -.
DR   Proteomes; UP000008141; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141}.
FT   DOMAIN          43..208
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   476 AA;  50498 MW;  35A4DC51EE08692B CRC64;
     MGLELEGIET LRAELRGRLL LPSEAAFTQA TSVWSVSPNH PARLPAPALV VQPRGTADVS
     AAVKFAAAHG LPLAGNPSWV DGGLMIDLSL MRRWRCVYVD PGAKTAVVDG GALACDVDAE
     TALHGLAAPL GVCCVVGMGL VLNGGISLLS RAHGPACDSI LGAQVVLADG SVVNVTSGGP
     DPDLFWALRG AGSTLGVVTK LTLQLYDAPT YSGAFVWRDD PEHATFKSVL RWIRAVVLPD
     PAVGFNCARM VHPELGPVLI SMLVIVGDRP VEEKEALVQP LRELGPIQAS DSVGRSSWHQ
     TQLTHYEAVT GLAQAFPVHY EAWSGGHVAA EKFTDEFIDA YVRCTADELP LPDCALTLAV
     LEVMGGKLRE SRAPVGLNEA DLQWVVQAGW ADAAAHETGK AYAQRLRSVL GPLSTSMGRY
     VNLLDVAEDP EMSYEEAATK AAGPANLERL RAVKAKYDPA GVFRNTPFMK VLAVKP
//
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