ID M1BW87_SOLTU Unreviewed; 530 AA.
AC M1BW87;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN Name=102593264 {ECO:0000313|EnsemblPlants:PGSC0003DMT400054387};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400054387, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400054387}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400054387};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00034114}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR RefSeq; XP_006352996.1; XM_006352934.2.
DR AlphaFoldDB; M1BW87; -.
DR STRING; 4113.M1BW87; -.
DR PaxDb; 4113-PGSC0003DMT400054387; -.
DR EnsemblPlants; PGSC0003DMT400054387; PGSC0003DMT400054387; PGSC0003DMG400021109.
DR GeneID; 102593264; -.
DR Gramene; PGSC0003DMT400054387; PGSC0003DMT400054387; PGSC0003DMG400021109.
DR KEGG; sot:102593264; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; M1BW87; -.
DR OMA; MTIQANF; -.
DR OrthoDB; 1094055at2759; -.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
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 GO; GO:0042179; P:nicotine biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF61; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..530
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004012265"
FT DOMAIN 71..245
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 530 AA; 60089 MW; C5E8188D383DB204 CRC64;
MTTFKKLTIF LFLSVCLSSS WANTTLHDDF LECLSHKIMN SNSISQVIYT PKNSSYSTLY
NSFSSNLRIT SDFKPSIIFT PNDESQIQAA IYCSKKHGLQ IRIRGGGHDY EGLSYISETP
FVIIDLRNLR SISIDTEDKT AWIQAGATLG EVYYRIAEKS KKLAFVAGVC PTVGVGGHFS
GGGYGMMSRK FGTAADNIID AKLIDANGRI LDRKSMGEDL FWAIRGGGGT SFGLIISWKV
KLLDIPEKVT VFNVTRTLEQ NATQLVYKWQ YIADKVDDNL LLRVFLGSSE SPFQRGQRTV
HAFFTTMFVG GVDDLLHEMQ DSFPELGLVK EDCIEMSWIE SILFFVGFPR GTSIDVLLDW
NNSTYQTGFF KGKSDYVQRP ISINGLEGIW KLFNQVGEYS AELQFSPYGG KLSDISQSET
PFPHRDGNIF MIHYGVNWRE MESSNKHLSW IRNLYGYMAR YVSKSPRAAY FNYRDLDLGV
NNKGNTSYEQ ARIWGVKYFK NNFDRLVKIK TKIDPTNFFR NEQSIPPLLS
//
