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Database: UniProt
Entry: D7SHL6_VITVI
LinkDB: D7SHL6_VITVI
Original site: D7SHL6_VITVI 
ID   D7SHL6_VITVI            Unreviewed;       473 AA.
AC   D7SHL6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Alliinase C-terminal domain-containing protein {ECO:0000259|Pfam:PF04864};
GN   OrderedLocusNames=VIT_17s0000g08990 {ECO:0000313|EMBL:CBI14976.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI14976.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the alliinase family.
CC       {ECO:0000256|ARBA:ARBA00006312}.
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DR   EMBL; FN594950; CBI14976.3; -; Genomic_DNA.
DR   RefSeq; XP_002281408.1; XM_002281372.3.
DR   AlphaFoldDB; D7SHL6; -.
DR   STRING; 29760.D7SHL6; -.
DR   PaxDb; 29760-VIT_17s0000g08990-t01; -.
DR   EnsemblPlants; Vitvi17g00889_t001; Vitvi17g00889_P001; Vitvi17g00889.
DR   GeneID; 100262049; -.
DR   Gramene; Vitvi17g00889_t001; Vitvi17g00889_P001; Vitvi17g00889.
DR   KEGG; vvi:100262049; -.
DR   eggNOG; ENOG502QPYC; Eukaryota.
DR   HOGENOM; CLU_036760_1_0_1; -.
DR   InParanoid; D7SHL6; -.
DR   OMA; HNILTRG; -.
DR   OrthoDB; 1275724at2759; -.
DR   Proteomes; UP000009183; Chromosome 17.
DR   ExpressionAtlas; D7SHL6; baseline and differential.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:amino acid metabolic process; IBA:GO_Central.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.10.25.30; EGF-like, alliinase; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR006948; Alliinase_C.
DR   InterPro; IPR037029; Alliinase_N_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43795:SF123; TRYPTOPHAN AMINOTRANSFERASE-RELATED PROTEIN 2; 1.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          101..460
FT                   /note="Alliinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04864"
FT   REGION          67..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  52879 MW;  529A2E4F921CEA43 CRC64;
     MKHIEGYLRV SLFLSEMGKL SGVFSLRHFL VLSLALNVAL ISRVVYEGEN WREEQIRALM
     ADASEKSAHV SMSSPPPPSP STPSSMAVTS TEIKDDGERV INLDHGDPTM YERFWQQMGD
     ITTIVISGWQ SMSYFSDVKN LCWFLEPEFA KQIIRLHKIV GNAVTDNYYI VVGTGSTQLF
     QAALYALSPP NASEPMSVVS AAPFYSSYPS VTDFLKSGLY KWAGDANNFN KDGPYIELVT
     SPNNPDGSIR QPVVNRSGEN LVHDFAYYWP QYTPISSPAD HDLMLFTVSK ATGHAGMRLG
     WALVKDKEVA KKMTSFIELN TIGVSKDSQQ RAAKILQVIS DSYEPVGNPK QSGPFFHFSH
     SMMEERWKAL RSAVKQSGLF SLPEFPSSFC NFLGQAFGSQ PAFAWLKCEG GIEDCGNFLK
     RHKILTRNGK HFGASPEYVR VSMLDRDESF NLFTKRLSSL HLSQSKDHEK ESP
//
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