PAMT_CAPCH
ID PAMT_CAPCH Reviewed; 459 AA.
AC O82521; A0A2G3CTB3; A0A6J3ZXX9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Vanillin aminotransferase {ECO:0000303|PubMed:24712445};
DE EC=2.6.1.119 {ECO:0000269|PubMed:24712445};
DE AltName: Full=Putative aminotransferase {ECO:0000303|Ref.1};
DE Short=pAMT;
GN Name=VAMT {ECO:0000303|PubMed:24712445};
OS Capsicum chinense (Scotch bonnet) (Bonnet pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=80379;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Habanero;
RA Aluru M., Curry J., O'Connell M.;
RT "Nucleotide Sequence of a Probable Aminotransferase Gene (Accession No.
RT AF085149) from Habanero Chile. (PGR98-182).";
RL Plant Physiol. 118:1102-1102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX DOI=10.1007/s11032-015-0339-9;
RA Tanaka Y., Sonoyama T., Muraga Y., Koeda S., Goto T., Yoshida Y.,
RA Yasuba K.;
RT "Multiple loss-of-function putative aminotransferase alleles contribute to
RT low pungency and capsinoid biosynthesis in Capsicum chinense.";
RL Mol. Breed. 35:142-142(2015).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=31323150; DOI=10.1111/tpj.14462;
RA Tanaka Y., Asano T., Kanemitsu Y., Goto T., Yoshida Y., Yasuba K.,
RA Misawa Y., Nakatani S., Kobata K.;
RT "Positional differences of intronic transposons in pAMT affect the pungency
RT level in chili pepper through altered splicing efficiency.";
RL Plant J. 100:693-705(2019).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI159236;
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19473323; DOI=10.1111/j.1365-313x.2009.03921.x;
RA Lang Y., Kisaka H., Sugiyama R., Nomura K., Morita A., Watanabe T.,
RA Tanaka Y., Yazawa S., Miwa T.;
RT "Functional loss of pAMT results in biosynthesis of capsinoids,
RT capsaicinoid analogs, in Capsicum annuum cv. CH-19 Sweet.";
RL Plant J. 59:953-961(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20973559; DOI=10.1021/jf1019642;
RA Tanaka Y., Hosokawa M., Miwa T., Watanabe T., Yazawa S.;
RT "Novel loss-of-function putative aminotransferase alleles cause
RT biosynthesis of capsinoids, nonpungent capsaicinoid analogues, in mildly
RT pungent chili peppers (Capsicum chinense).";
RL J. Agric. Food Chem. 58:11762-11767(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24712445; DOI=10.1186/1472-6750-14-25;
RA Weber N., Ismail A., Gorwa-Grauslund M., Carlquist M.;
RT "Biocatalytic potential of vanillin aminotransferase from Capsicum
RT chinense.";
RL BMC Biotechnol. 14:25-25(2014).
CC -!- FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent
CC cultivars of Capsicum chinense (Ref.2, PubMed:31323150). Capsaicinoids,
CC the alkaloids responsible for the heat or pungency of chili pepper, are
CC synthesized from phenylpropanoid intermediates in the placental tissue
CC of chili peper fruit (Probable). Can transfer an amine from
CC vanillylamine to pyruvate forming vanillin and L-alanine
CC (PubMed:24712445). Can use pyruvate or oxaloacetate, but not 2-
CC oxoglutarate as amino group acceptors (PubMed:24712445). Is able to
CC convert (S)-1-phenylethylamine into acetophenone in vitro
CC (PubMed:24712445). {ECO:0000269|PubMed:24712445,
CC ECO:0000269|PubMed:31323150, ECO:0000269|Ref.2, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine + vanillin = pyruvate + vanillylamine;
CC Xref=Rhea:RHEA:63828, ChEBI:CHEBI:15361, ChEBI:CHEBI:18346,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:149596; EC=2.6.1.119;
CC Evidence={ECO:0000269|PubMed:24712445};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:24712445};
CC -!- TISSUE SPECIFICITY: Expressed in placental tissue of immature fruit.
CC {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Low pungency phenotype, characterized by low
CC levels of capsaicinoids, and accumulation of high levels of capsinoids,
CC which are non-pungent capsaicinoid analogs.
CC {ECO:0000269|PubMed:19473323, ECO:0000269|PubMed:20973559,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF085149; AAC78480.1; -; mRNA.
DR EMBL; LC032106; BAU36962.1; -; Genomic_DNA.
DR EMBL; LC483648; BBK20873.1; -; Genomic_DNA.
DR EMBL; LC483649; BBK20874.1; -; Genomic_DNA.
DR EMBL; MCIT02000003; PHU21971.1; -; Genomic_DNA.
DR AlphaFoldDB; O82521; -.
DR SMR; O82521; -.
DR STRING; 80379.A0A2G3CTB3; -.
DR OrthoDB; 145181at2759; -.
DR BioCyc; MetaCyc:MON-13529; -.
DR BRENDA; 2.6.1.119; 11996.
DR Proteomes; UP000224522; Chromosome 3.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:UniProtKB.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Coiled coil; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..459
FT /note="Vanillin aminotransferase"
FT /id="PRO_0000451917"
FT COILED 428..459
FT /evidence="ECO:0000255"
FT BINDING 115..116
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 320..321
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT CONFLICT 125
FT /note="L -> M (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="T -> A (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="Y -> H (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="G -> S (in Ref. 1; AAC78480, 2; BAU36962 and 3;
FT BBK20873/BBK20874)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> G (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="M -> I (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="K -> Q (in Ref. 1; AAC78480 and 2; BAU36962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50769 MW; 026A492DF98DBDC9 CRC64;
MANITNEFMG HDMLAPFTAG WQSDMEPLVI EKSEGSYVYD INGKKYLDTL SGLWCATLGG
SETRLVEAAN KQLNTLPFYH SFWNRTTKPS LDLAKELLNM FTANKMAKVF FTNSGSEAND
TQVKLVWYYN NALGRPQKKK IIARAKAYHG STYISAGLSG LPPMHQKFDL PPPFVLHTEC
PHYWAYHLPG ETEEEFSTRL ANNLESLILK EGPETVAAFI AEPVLGAAGV ILPPATYFDK
VQTILRKYDI LFIADEVVCG FGRLGTMFGG DKYNIKPDLV SVAKALSSGY MPIAAVLVSQ
KISSVILSES NKIGAFCHGF TYSGHPVACA VALEALKIYK ERNITEVVNK ISQKFQEGLK
AFADSPIIGE IRGTGLALST EFVDNKSPND PFPYEWAVGT YFGAQCAKYG MLVSSTGDHV
NMAPPFMLSL EELDELIRIY GKALKDTEKR VEELKSQKK
