ID   NAATB_HORVU             Reviewed;         551 AA.
AC   Q9ST03; Q9ST44;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Nicotianamine aminotransferase B {ECO:0000312|EMBL:BAA87053.1};
DE            EC=2.6.1.80;
GN   Name=naat-B {ECO:0000312|EMBL:BAA87054.1};
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:BAA87054.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Ehimehadaka No.1 {ECO:0000269|PubMed:10557244};
RC   TISSUE=Root {ECO:0000312|EMBL:BAA87053.1};
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. Only a trace amount of expression is
CC       detected when sufficient iron is present.
CC       {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; AB005788; BAA87053.1; -; mRNA.
DR   EMBL; AB024006; BAA87054.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ST03; -.
DR   SMR; Q9ST03; -.
DR   PRIDE; Q9ST03; -.
DR   KEGG; ag:BAA87053; -.
DR   BioCyc; MetaCyc:MON-13947; -.
DR   BRENDA; 2.6.1.80; 2687.
DR   ExpressionAtlas; Q9ST03; 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   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..551
FT                   /note="Nicotianamine aminotransferase B"
FT                   /id="PRO_0000405351"
FT   REGION          24..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         379
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04694"
FT   CONFLICT        198
FT                   /note="V -> L (in Ref. 1; BAA87054)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  58149 MW;  54DC78358408371C CRC64;
     MATVRQSDGV AANGLAVAAA ANGKSNGHGV AAAVNGKSNG HGVDADANGK SNGHGVAADA
     NGKSNGHAEA TANGHGEATA NGKTNGHRES NGHAEAADAN GESNEHAEDS AANGESNGHA
     AAAAEEEEAV EWNFAGAKDG VLAATGANMS IRAIRYKISA SVQEKGPRPV LPLAHGDPSV
     FPAFRTAVEA EDAVAAAVRT GQFNCYPAGV GLPAARSAVA EHLSQGVPYM LSADDVFLTA
     GGTQAIEVII PVLAQTAGAN ILLPRPGYPN YEARAAFNRL EVRHFDLIPD KGWEIDIDSL
     ESIADKNTTA MVIINPNNPC GSVYSYDHLS KVAEVAKRLG ILVIADEVYG KLVLGSAPFI
     PMGVFGHITP VLSIGSLSKS WIVPGWRLGW VAVYDPRKIL QETKISTSIT NYLNVSTDPA
     TFIQAALPQI LENTKEDFFK AIIGLLKESS EICYKQIKEN KYITCPHKPE GSMFVMVKLN
     LHLLEEIDDD IDFCCKLAKE ESVILCPGSV LGMANWVRIT FACVPSSLQD GLGRIKSFCQ
     RNKKRNSSDD C