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Database: UniProt
Entry: A0A251VAY5_HELAN
LinkDB: A0A251VAY5_HELAN
Original site: A0A251VAY5_HELAN 
ID   A0A251VAY5_HELAN        Unreviewed;       530 AA.
AC   A0A251VAY5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000313|EMBL:KAF5810082.1};
DE            EC=4.4.1.14 {ECO:0000313|EMBL:KAF5810082.1};
DE   SubName: Full=Putative ACC synthase 10 {ECO:0000313|EMBL:OTG32604.1};
GN   Name=ACS10 {ECO:0000313|EMBL:OTG32604.1};
GN   ORFNames=HannXRQ_Chr03g0088501 {ECO:0000313|EMBL:OTG32604.1},
GN   HanXRQr2_Chr04g0165191 {ECO:0000313|EMBL:KAF5810082.1};
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:OTG32604.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5810082.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5810082.1};
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).
RN   [2] {ECO:0000313|EMBL:OTG32604.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG32604.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5810082.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5810082.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; MNCJ02000319; KAF5810082.1; -; Genomic_DNA.
DR   EMBL; CM007892; OTG32604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251VAY5; -.
DR   STRING; 4232.A0A251VAY5; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr04g0165191; mRNA:HanXRQr2_Chr04g0165191; HanXRQr2_Chr04g0165191.
DR   Gramene; mRNA:HanXRQr2_Chr04g0165191; mRNA:HanXRQr2_Chr04g0165191; HanXRQr2_Chr04g0165191.
DR   InParanoid; A0A251VAY5; -.
DR   OMA; MYGSEEF; -.
DR   OrthoDB; 1328656at2759; -.
DR   Proteomes; UP000215914; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProt.
DR   GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43795:SF117; ACC SYNTHASE 10-RELATED; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KAF5810082.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..519
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  58462 MW;  3DE98BDD41FF3F81 CRC64;
     MTQTGPRRLR NSALDDDSQP QPQPQPSSST TGMRLIVPLQ GIVQGRGGLI LGSVIPCAMF
     YFLQFYLKRR RSPPASNPPS PGNLTDLSRS ASRSNLLLPR GRPHVSSRVS SIAKANDSPY
     YIGLDKATSD PYDRLCNPGG VVQLGLAENR LTLDLIENWI TNNLNESILG GGLSVSGIVT
     YQPHDGMPEL KLAMAGLMSQ VVGKTVTFNP SQIVLTSGAT PAIEILCFAL ADQGNTFLIP
     APYYPGFDRD MKWRTGVELI PVHCRSSDNF TLSIPVLEQA FNQARKRGQK VKGILLSNPS
     NPVGNLMTRE TLLSLLDFAR EKNIHIISDE IFSGSTFGDE EFVSMAEIID SEDADKDRVH
     IVYGLSKDLS LPGFRVGVIY SYNENVLTVA RKMTRFSSVS APTQRLVTSM LSDTTFIKSY
     TERNRERLRT MYDLFVDGLK ELGIGCTKSS GGLYCWCDMS GLIRPYNEKG ELDLWDKLLN
     VGKINITPGS SCHCIEPGWF RCCFTTLDEN DIPVVMERIR LVVEACKSPA
//
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