ID D7MMH7_ARALL Unreviewed; 354 AA.
AC D7MMH7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ARALYDRAFT_356638 {ECO:0000313|EMBL:EFH39842.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; GL348720; EFH39842.1; -; Genomic_DNA.
DR RefSeq; XP_002863583.1; XM_002863537.1.
DR AlphaFoldDB; D7MMH7; -.
DR STRING; 81972.D7MMH7; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_8000425; fgenesh1_pg.C_scaffold_8000425; fgenesh1_pg.C_scaffold_8000425.
DR Gramene; fgenesh1_pg.C_scaffold_8000425; fgenesh1_pg.C_scaffold_8000425; fgenesh1_pg.C_scaffold_8000425.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR32448:SF94; BERBERINE BRIDGE ENZYME-LIKE 24-RELATED; 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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
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:UP000008694};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..170
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 354 AA; 40887 MW; 819D8789F8C6C521 CRC64;
MPKPGFIFRP IHESQVQASI ICSKKLGIHF RVRSGGHDFE ALSYVSRIEK PFILLDMSKL
RQITVDIKDN SAWVQPGATL GELYYRRKLV PVPETLTVFT VTKTLKQDAR LKIISKWQRI
ASKLIEELHI RVELRAIGNN GNKTVTMSYK GQFLGKKGIL MKVMKKAFPE LGLTQEDCIE
MSWIESTLFG GGFPTGSPIE VLLQVKSPLG KGYFKATRDA PFLNWTPYGG MMAKIPESEI
PFPHRNGTLF KILYQTNWQE NDKRQSRHIN WIKEMYSYMA PYVSSNPRQA YVNYRDLDFG
QNRNNSKVNF IEAKIWGAKY FKDNFNRLVR IKTKVDPDNF FRHEQSIPTL PVRS
//
