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Database: UniProt
Entry: A0A1S2YNL3_CICAR
LinkDB: A0A1S2YNL3_CICAR
Original site: A0A1S2YNL3_CICAR 
ID   A0A1S2YNL3_CICAR        Unreviewed;       580 AA.
AC   A0A1S2YNL3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=(R)-mandelonitrile lyase-like {ECO:0000313|RefSeq:XP_004507539.1};
GN   Name=LOC101508164 {ECO:0000313|RefSeq:XP_004507539.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004507539.1};
RN   [1] {ECO:0000313|RefSeq:XP_004507539.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004507539.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_004507539.1; XM_004507482.3.
DR   AlphaFoldDB; A0A1S2YNL3; -.
DR   STRING; 3827.A0A1S2YNL3; -.
DR   PaxDb; 3827-XP_004507539-1; -.
DR   GeneID; 101508164; -.
DR   KEGG; cam:101508164; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca6.
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:SF2; (R)-MANDELONITRILE LYASE-LIKE; 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; 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};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Lyase {ECO:0000313|RefSeq:XP_004507539.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          313..327
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         92..93
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         144
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         259
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         514..515
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         543
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         554..555
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        455..506
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   580 AA;  63745 MW;  D522C5A9A9A7D9D3 CRC64;
     MEKSAITVTT EFLFLTSFIT IFIGSAFASP TQNQESNSQE QQDKPPSYLR MVANASEFPL
     EDYYDYIIVG GGTAGCPLAA TLSQNYRVLV LERGGVTHGK SNLMNQEGFL NTLLNANVNN
     ANNEDSPAQS FISEDGVLNA RGRVLGGSSA INAGFYSRAD HEFFTRSGVI WDSKLVNESY
     EWVEREIVFR PQLKTWQSAF RDGLLEARVG PYNGFTLDHA TGTKIGGSTF DTSGKRHSSA
     DLLRYARHSN LRIAVYASVE RILLASSSSS TTTSSETSSS ATTSAIGVLY RDQNGKYHHA
     ILRGRGEVIL AAGAIGSPQL LLLSGIGPRP YLSSWGIPVT HHLPYVGHFL YDNPRNGITF
     LPSIPLEHSL IQVVGITNSG AYIEAASNVV PFSSPVRNFF IRESNSPLYL TVATLISKIS
     GPVSAGFLRL ASTDVRFNPI VRFNYFNNGV DVERCVNGTR KLGEVLRSRA MNDFKFVNWL
     GVRDFRFIGP ALPNDESDYI EMADFCRRTV STIWHYHGGC VVGRVVDSHL KVIGIDSLRI
     VDGSVFSVSP GTNPQATLMM LGRYFGLKMI REREGYSNDL
//
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