ID I1K2W8_SOYBN Unreviewed; 547 AA.
AC I1K2W8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, 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 Name=100780114 {ECO:0000313|EnsemblPlants:KRH58388};
GN ORFNames=GLYMA_05G124900 {ECO:0000313|EMBL:KRH58388.1};
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:KRH58388};
RN [1] {ECO:0000313|EMBL:KRH58388.1, ECO:0000313|EnsemblPlants:KRH58388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH58388};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH58388.1};
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:KRH58388}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH58388};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH58388.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH58388.1};
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; CM000838; KRH58388.1; -; Genomic_DNA.
DR RefSeq; XP_003524099.2; XM_003524051.3.
DR AlphaFoldDB; I1K2W8; -.
DR SMR; I1K2W8; -.
DR STRING; 3847.I1K2W8; -.
DR PaxDb; 3847-GLYMA05G25460-1; -.
DR EnsemblPlants; KRH58388; KRH58388; GLYMA_05G124900.
DR GeneID; 100780114; -.
DR Gramene; KRH58388; KRH58388; GLYMA_05G124900.
DR KEGG; gmx:100780114; -.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; I1K2W8; -.
DR OMA; WEGRLAN; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000008827; Chromosome 5.
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; OS08G0158400 PROTEIN; 1.
DR PANTHER; PTHR32448:SF170; RETICULINE OXIDASE-LIKE 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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..547
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014577471"
FT DOMAIN 83..257
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 547 AA; 61135 MW; 2796759146064EAB CRC64;
MHNNTPSTKM MRLSSYFVVA IALLFSFTPS SSANTHENFV QCLYNYPHNN NVTSISNVVY
TQANSSYSSI LDFSIQNLRF SNASSKPLVI VTPLTVSHIQ ATIICSQRYG MQIRTRSGGH
DYEGLSYVAK DPFVVLDLIN LRKIEVDAEN STAWVLAGAT IGELYYSISQ KSKTLGFPAG
VCPPVGTGGH FSGGGYGFLM RKFGLAADNV IDAHIVDVKG NLLDREAMGE DLFWAIRGGG
GASFGVIVAW KIKLVSVPST VTVFRVPRTL EQNATEIVHK WQLVANKLDE DLTIRINFGR
ATSENGNLTV QAQFESMYLG GVDQLIPLMQ ESFPELGLVR EDCIETSWIG SILYMAGFTN
GESTDVLLNR TQANGVSFNK GKSDYVRDPI PDVGLEGLWP FFFEDEGQSS FVQFTPYGSR
MDEISESEIP FPHRAGNIFH IQYGVSWQEE GDEEAQRHIN WIRRMYSYME TYVSKSPRAA
YLNYRDLDIG VNNNKGYTSY SQASVWGLKY FKNNFNRLAR VKTNVDPLNF FRNEQSIPSL
VSKGRKL
//
