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Database: UniProt
Entry: B9I0Y5_POPTR
LinkDB: B9I0Y5_POPTR
Original site: B9I0Y5_POPTR 
ID   B9I0Y5_POPTR            Unreviewed;       545 AA.
AC   B9I0Y5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=POPTR_011G158700 {ECO:0000313|EMBL:PNT13734.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT13734.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT13734.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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; CM009300; PNT13734.1; -; Genomic_DNA.
DR   RefSeq; XP_002317089.1; XM_002317053.2.
DR   AlphaFoldDB; B9I0Y5; -.
DR   STRING; 3694.B9I0Y5; -.
DR   EnsemblPlants; Potri.011G158700.1.v4.1; Potri.011G158700.1.v4.1; Potri.011G158700.v4.1.
DR   GeneID; 7489117; -.
DR   Gramene; Potri.011G158700.1.v4.1; Potri.011G158700.1.v4.1; Potri.011G158700.v4.1.
DR   KEGG; pop:7489117; -.
DR   eggNOG; ENOG502QQWK; Eukaryota.
DR   HOGENOM; CLU_018354_6_0_1; -.
DR   InParanoid; B9I0Y5; -.
DR   OMA; MRQVNIN; -.
DR   OrthoDB; 1094055at2759; -.
DR   Proteomes; UP000006729; Chromosome 11.
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; PTHR32448:SF35; BERBERINE BRIDGE ENZYME-LIKE 13; 1.
DR   PANTHER; PTHR32448; OS08G0158400 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..545
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030166274"
FT   DOMAIN          72..250
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          524..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  60882 MW;  161F5DB930938D12 CRC64;
     MVPSSFCIFS TLVVLLLSSS VTVSLPIKDD FVQCFLQNSE ISVPTSSFYT PDNSSSFSAV
     LQSTAQNLRY LLPSVPKPVF IFTPLYEAHV QASVICCRQL GLHLRVRSGG HDYEGLSYAS
     EIESPFIVVD LAKLRAIQVN IEDNSAWVQA GATIGELYYR IAEKSKTHGF PAGLCSSLGI
     GGHITGGAYG SMMRKYGLGA DNVIDARVID ASGRVLERQS MGEDFFWAIR GGGGASFGII
     TAWKVKLVPV PSTVTVFTVT KTLEQGGTKL LYRWQQVADK LDEDLFIRVI IQTANGAKKG
     QRTVTTSYNA LFLGDASRLL NVMKTGFPEL GLTRKDCVET TWLKSVLYIA GYPANTPPEV
     LLQGKSTFKN YFKAKSDFVQ HPIPEAALEG IWKRYFQEVT PFMIWNPYGG MMSKISESSI
     PFPHRKGVLF KIQYLTSWQT PAEDASKHIN WIRKLYKYMA PYVSMFPRQA YVNYRDLDLG
     MNKKRNTSFK EASVWGTKYF KNNFNRLVQV KTTVDPDNFF RHEQSIPPLP LSSRKGKGKG
     HHGIH
//
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