ID I1KRB4_SOYBN Unreviewed; 539 AA.
AC I1KRB4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN Name=100796809 {ECO:0000313|EnsemblPlants:KRH42272};
GN ORFNames=GLYMA_08G080500 {ECO:0000313|EMBL:KRH42272.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH42272};
RN [1] {ECO:0000313|EMBL:KRH42272.1, ECO:0000313|EnsemblPlants:KRH42272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH42272};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42272.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH42272}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH42272};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH42272.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42272.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000841; KRH42272.1; -; Genomic_DNA.
DR RefSeq; XP_003531066.1; XM_003531018.3.
DR AlphaFoldDB; I1KRB4; -.
DR SMR; I1KRB4; -.
DR STRING; 3847.I1KRB4; -.
DR PaxDb; 3847-GLYMA08G08530-1; -.
DR EnsemblPlants; KRH42272; KRH42272; GLYMA_08G080500.
DR GeneID; 100796809; -.
DR Gramene; KRH42272; KRH42272; GLYMA_08G080500.
DR KEGG; gmx:100796809; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; I1KRB4; -.
DR OMA; WWANYND; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000008827; Chromosome 8.
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:SF34; BERBERINE BRIDGE ENZYME-LIKE 19-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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..539
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014577784"
FT DOMAIN 79..253
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 539 AA; 60405 MW; 4EC4025587DC91D0 CRC64;
MEKSNSLPFL SVIVLLLHVS NSLTTPTRES IHDTFLHCLQ SHTTNQPDHV SNIVYAQTNT
SYTSVLRAFA RNARFSAPST QKPLLIVTPL SENQVQATVV CAKSIGLQLK IRSGGHDFEG
VSYISQVPFI ILDMFNFQDV TVDVQNEIAV IQAGASLGQV YYRIWEKSKV HGFPAGACPT
VGVGGHLSGG GYGNMIRKYG LSVDHVVDAK IVDVKGRILD KESMGEDLFW AIRGGGGASF
GVILSYTVKL VPVPENVTVF QIDKTLEENA TDLVVQWQKV APHTDDRLYL RLVLQPVSSN
FVKGKKTIRA SVEALFLGEA DELVKLLGQE FPLLGLKKEL CHEMRWIDSV VWWANYNDGS
SVNALLDRNH YSVHSNKRKS DYVQTPISKD GFTWIWKKMI ELGKVSIVFN PYGGKMNEVP
SDATPFPHRA GNLYKIQYTV SWQEPGAAVE KSFLSQIRVL HNYMTPFVSK NPRSAYFNYR
DLDIGINSHG KDNFEDGKVY GIKYFNKNFE RLVKVKSAID PENFFWNEQS IPTYPRSNA
//