ID   NAATA_HORVU             Reviewed;         461 AA.
AC   Q9ST02; Q9SMG7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nicotianamine aminotransferase A {ECO:0000312|EMBL:BAA87052.2};
DE            EC=2.6.1.80;
DE   AltName: Full=Nicotianamine aminotransferase III {ECO:0000303|PubMed:10557244};
DE            Short=NAAT-III {ECO:0000303|PubMed:10557244};
GN   Name=naat-A {ECO:0000312|EMBL:BAA87055.1};
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA87055.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 33-47;
RP   222-232; 273-280 AND 385-403, FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Ehimehadaka No.1 {ECO:0000269|PubMed:10557244};
RC   TISSUE=Root {ECO:0000312|EMBL:BAA87052.2};
RX   PubMed=10557244; DOI=10.1104/pp.121.3.947;
RA   Takahashi M., Yamaguchi H., Nakanishi H., Shioiri T., Nishizawa N.K.,
RA   Mori S.;
RT   "Cloning two genes for nicotianamine aminotransferase, a critical enzyme in
RT   iron acquisition (Strategy II) in graminaceous plants.";
RL   Plant Physiol. 121:947-956(1999).
CC   -!- FUNCTION: Involved in biosynthesis of mugineic acid family
CC       phytosiderophores. {ECO:0000269|PubMed:10557244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + nicotianamine = 3''-deamino-3''-
CC         oxonicotianamine + L-glutamate; Xref=Rhea:RHEA:22104,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58249,
CC         ChEBI:CHEBI:58685; EC=2.6.1.80;
CC         Evidence={ECO:0000269|PubMed:10557244};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P04694};
CC   -!- TISSUE SPECIFICITY: Expressed in roots, but not in leaves.
CC       {ECO:0000269|PubMed:10557244}.
CC   -!- INDUCTION: By iron deficiency. No expression is detected when
CC       sufficient iron is present. {ECO:0000269|PubMed:10557244}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   EMBL; AB024006; BAA87055.1; -; Genomic_DNA.
DR   EMBL; D88273; BAA87052.2; -; mRNA.
DR   AlphaFoldDB; Q9ST02; -.
DR   SMR; Q9ST02; -.
DR   KEGG; ag:BAA87052; -.
DR   BioCyc; MetaCyc:MON-13945; -.
DR   BRENDA; 2.6.1.80; 2687.
DR   ExpressionAtlas; Q9ST02; baseline and differential.
DR   GO; GO:0033855; F:nicotianamine aminotransferase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR005958; TyrNic_aminoTrfase.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..461
FT                   /note="Nicotianamine aminotransferase A"
FT                   /id="PRO_0000405350"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         289
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04694"
FT   CONFLICT        402
FT                   /note="D -> N (in Ref. 1; BAA87055)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  49565 MW;  85326EA8F38B4449 CRC64;
     MVHQSNGHGE AAAAAANGKS NGHAAAANGK SNGHAAAAAV EWNFARGKDG ILATTGAKNS
     IRAIRYKISA SVEESGPRPV LPLAHGDPSV FPAFRTAVEA EDAVAAALRT GQFNCYAAGV
     GLPAARSAVA EHLSQGVPYK LSADDVFLTA GGTQAIEVII PVLAQTAGAN ILLPRPGYPN
     YEARAAFNKL EVRHFDLIPD KGWEIDIDSL ESIADKNTTA MVIINPNNPC GSVYSYDHLA
     KVAEVARKLG ILVIADEVYG KLVLGSAPFI PMGVFGHIAP VLSIGSLSKS WIVPGWRLGW
     VAVYDPTKIL EKTKISTSIT NYLNVSTDPA TFVQEALPKI LENTKADFFK RIIGLLKESS
     EICYREIKEN KYITCPHKPE GSMFVMVKLN LHLLEEIHDD IDFCCKLAKE ESVILCPGSV
     LGMENWVRIT FACVPSSLQD GLERVKSFCQ RNKKKNSING C