PAMT_CAPFR
ID PAMT_CAPFR Reviewed; 459 AA.
AC D6R3B6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Vanillin aminotransferase {ECO:0000303|PubMed:22921003};
DE EC=2.6.1.119 {ECO:0000269|PubMed:22921003};
DE AltName: Full=Putative aminotransferase {ECO:0000303|PubMed:22921003};
DE Short=pAMT {ECO:0000303|PubMed:22921003};
GN Name=PAMT {ECO:0000305};
OS Capsicum frutescens (Cayenne pepper) (Tabasco pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4073;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22921003; DOI=10.1016/j.plantsci.2012.06.014;
RA Gururaj H.B., Padma M.N., Giridhar P., Ravishankar G.A.;
RT "Functional validation of Capsicum frutescens aminotransferase gene
RT involved in vanillylamine biosynthesis using Agrobacterium mediated genetic
RT transformation studies in Nicotiana tabacum and Capsicum frutescens calli
RT cultures.";
RL Plant Sci. 195:96-105(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF 155-SER--LEU-158.
RX PubMed=26048129; DOI=10.1007/s00438-015-1071-1;
RA Park Y.J., Nishikawa T., Minami M., Nemoto K., Iwasaki T., Matsushima K.;
RT "A low-pungency S3212 genotype of Capsicum frutescens caused by a mutation
RT in the putative aminotransferase (p-AMT) gene.";
RL Mol. Genet. Genomics 290:2217-2224(2015).
CC -!- FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent
CC cultivars of Capsicum frutescens (PubMed:22921003, PubMed:26048129).
CC Capsaicinoids, the alkaloids responsible for the heat or pungency of
CC chili pepper, are synthesized from phenylpropanoid intermediates in the
CC placental tissue of chili peper fruit (Probable). Can transfer an amine
CC from alanine to vanillin, forming vanillylamine and pyruvate
CC (PubMed:22921003). {ECO:0000269|PubMed:22921003,
CC ECO:0000269|PubMed:26048129, 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:22921003};
CC -!- TISSUE SPECIFICITY: Expressed in placental tissue of immature fruit.
CC {ECO:0000269|PubMed:26048129}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; HM057189; ADG65346.1; -; mRNA.
DR EMBL; LC019771; BAR88386.1; -; mRNA.
DR EMBL; LC019772; BAR88387.1; -; mRNA.
DR AlphaFoldDB; D6R3B6; -.
DR SMR; D6R3B6; -.
DR BRENDA; 2.6.1.119; 1172.
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; Transferase.
FT CHAIN 1..459
FT /note="Vanillin aminotransferase"
FT /id="PRO_0000451918"
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 MUTAGEN 155..158
FT /note="Missing: Low pungency phenotype, characterized by
FT low levels of capsaicinoids, and accumulation of high
FT levels of capsinoids, which are non-pungent capsaicinoid
FT analogs."
FT /evidence="ECO:0000269|PubMed:26048129"
SQ SEQUENCE 459 AA; 50698 MW; D0F13FB8923C249F CRC64;
MANITNEFMG HDMLAPFTAG WQSDMEPLVI EKSKGSYVYD INGKKYLDTL SGLWCATLGG
SETRLVEAAN KQLNTLPFYH SFWNRTTKPS LDLAKELLNM FTANKMAKVF FTNSGSEAND
TQVKLVWYYN NALGRPQKKK IIARAKAYHG STYISAGLSG LPPMHQKFDL PPPFVLHTEC
PHYWAYHLPG ETEEEFSTRL ANNLESLILN EGPETVAAFI AEPVLGAAGV ILPPATYFDK
VQAILRKHDI LFIADEVVCG FGRLGTMFGS DKYNIKPDLV SVAKALSSGY MPIAAVLVSQ
KISSVILSES NKIGAFCHGF TYSGHPVACA VALEALKIYK ERNITEVVNK ISQKFQEGLK
AFADSPIIGE IRGTGLALST EFVDNKSPND PFPYEWAVGT YFGAQCAKYG MLVSSTGDHV
NMAPPFTLSL EELDELIRIY GKALKDTEKR VEELKSQKK
