ID A0A251TTE7_HELAN Unreviewed; 587 AA.
AC A0A251TTE7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative (R)-mandelonitrile lyase 2 {ECO:0000313|EMBL:OTG14039.1};
GN Name=MDL2 {ECO:0000313|EMBL:OTG14039.1};
GN ORFNames=HannXRQ_Chr09g0244931 {ECO:0000313|EMBL:OTG14039.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG14039.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CM007898; OTG14039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251TTE7; -.
DR STRING; 4232.A0A251TTE7; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr09g0371901; mRNA:HanXRQr2_Chr09g0371901; HanXRQr2_Chr09g0371901.
DR Gramene; mRNA:HanXRQr2_Chr09g0371901; mRNA:HanXRQr2_Chr09g0371901; HanXRQr2_Chr09g0371901.
DR InParanoid; A0A251TTE7; -.
DR OMA; FFGIAYR; -.
DR Proteomes; UP000215914; Chromosome 9.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR45968:SF37; (R)-MANDELONITRILE LYASE 4-RELATED; 1.
DR PANTHER; PTHR45968; OSJNBA0019K04.7 PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Lyase {ECO:0000313|EMBL:OTG14039.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 161..184
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 320..334
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 521..522
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 561..562
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 462..513
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 587 AA; 64427 MW; 32F6D345CC4530A5 CRC64;
MLQLLLTYIT KRVLLTPSHS IYLSIYLSLC SNNNMKKVNH ELLAVFLLVI CVRLQWKIEC
FLEPNSHSDD SYLGFTHEAT DFTPEEAYDY IIVGGGTAGC PLAATLSEKY SVLLLERGGV
ASSDPNIVYE DRMLNPILYT NPFDSPAQSF ITEDGVLNFR GRVLGGTSMI NFGFYSRGDD
YFYQNSGIEW DMSAVNSAYE WVENSIVTRT DHLRRWQAST YNAFVEAGVG PGNGFILDHV
QGTKIGGSTF DDSGIRHGAV ELLSKANPDN LKVVVHAIVD RVIFSTSEPL AATGVRYHDS
NGTRHEVHVR TGGEVILSAG AIGSPQLLLL SGLGPNSSLL SLNIPVVRDH PFVGQFMADN
PRNSINLLVP VRLTDVGVRV AGITNSGPYV ESLAIPRVTS LIPFIPNLNL IPPANLSVVV
FGGKVSRPKS TGSLNLISSF DVTVGPRVRF NYYSNTADLL QCRNIVDVFR NVLETQAMEE
YKFPSIIGPR RFSYIGPSIP TDSSDEESIA TFCRQTLATF WHHHGGCLVN KVVDSHLKVI
GVDSLRVVDA STYFNAPGTN PQATTMMLGR YIAEKIVNER AAQNNHS
//
