ID A0A0D2N6F3_GOSRA Unreviewed; 541 AA.
AC A0A0D2N6F3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=B456_001G069600 {ECO:0000313|EMBL:KJB08183.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB08183.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB08183.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CM001740; KJB08183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2N6F3; -.
DR STRING; 29730.A0A0D2N6F3; -.
DR EnsemblPlants; KJB08183; KJB08183; B456_001G069600.
DR Gramene; KJB08183; KJB08183; B456_001G069600.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR OMA; QPDEIWS; -.
DR Proteomes; UP000032304; Chromosome 1.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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:SF13; BERBERINE BRIDGE ENZYME-LIKE B; 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 Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..541
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002247842"
FT DOMAIN 69..245
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 541 AA; 60001 MW; 8DF02F6E5A207414 CRC64;
MVNLSLLLLH FLISSLSVSG SAATDQRNIM SCLNYYNISN YTISSNVHNH DYSILLNFSI
QNLRFAEPTI PKPIAIILPE NKEQLINTVV CCTKGPWEIR VRCGGHSYEG TSSVASDGAP
FVIIDMMNLN RVSVDLGNET AWVEGGATLG ETYHAIAESS FIHGFAAGSC PTVGTGGHIG
GGGFGFLSRK YGLAADNVID ALLLNAEGEL LDRQAMGEDV FWAIRGGGGG IWGIVYAWKI
KLLRVPKTVT SFIVSRPGTK AHVANLVNKW QHVAPNLEGD MYLSCAVGAG LPQAKSIGIS
ATFNGFFLGR KREAVLILRR VFAELGVAEE DCKEMSWIES VLFFSGLGDG ALVSDLKNRY
LHDKHYFKAK SDYVRNPISL TGIRTAIDIL EKQPRGYIIM DPYGGIMNNI SNDSIAFPHR
YGNLYTIQYL VEWHQEEKNR SNEYREWIRD FYDAMASHVS WGPRAAYVNY MDFDLGVMEL
INTSVLSEDT VEMARVWGEK YFLNNYDRLV KAKTLIDPNN VFKNQQGIPP STTIGLKART
F
//
