ID   NAS8_HORVU              Reviewed;         329 AA.
AC   Q9XFB6;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Nicotianamine synthase 8;
DE            EC=2.5.1.43;
DE   AltName: Full=S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 8;
GN   Name=NAS8; Synonyms=NASHOR1;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-118 AND 255-263, AND
RP   FUNCTION.
RC   STRAIN=cv. Bonus;
RX   PubMed=10491178; DOI=10.1046/j.1432-1327.1999.00717.x;
RA   Herbik A., Koch G., Mock H.-P., Dushkov D., Czihal A., Thielmann J.,
RA   Stephan U.W., Baeumlein H.;
RT   "Isolation, characterization and cDNA cloning of nicotianamine synthase
RT   from barley. A key enzyme for iron homeostasis in plants.";
RL   Eur. J. Biochem. 265:231-239(1999).
CC   -!- FUNCTION: Synthesizes nicotianamine, a polyamine that is the first
CC       intermediate in the synthesis of the phytosiderophores of the mugineic
CC       acid type found in gramineae which serve as a sensor for the
CC       physiological iron status within the plant, and/or might be involved in
CC       the transport of iron. {ECO:0000269|PubMed:10491178}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-
CC         methyl-5'-thioadenosine; Xref=Rhea:RHEA:16481, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17509, ChEBI:CHEBI:58249, ChEBI:CHEBI:59789; EC=2.5.1.43;
CC   -!- SUBUNIT: Homotrimer.
CC   -!- INDUCTION: Fivefold increase after iron deficiency.
CC   -!- SIMILARITY: Belongs to the nicotianamine synthase (NAS)-like family.
CC       {ECO:0000305}.
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DR   EMBL; AF136941; AAD32650.1; -; mRNA.
DR   AlphaFoldDB; Q9XFB6; -.
DR   SMR; Q9XFB6; -.
DR   BRENDA; 2.5.1.43; 2687.
DR   GO; GO:0030410; F:nicotianamine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030418; P:nicotianamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR004298; Nicotian_synth.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR32266; PTHR32266; 1.
DR   Pfam; PF03059; NAS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51142; NAS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..329
FT                   /note="Nicotianamine synthase 8"
FT                   /id="PRO_0000212711"
FT   CONFLICT        118
FT                   /note="R -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255..256
FT                   /note="GG -> LE (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  35480 MW;  F12158E2F1BF819B CRC64;
     MDAQNKEVDA LVQKITGLHA AIAKLPSLSP SPDVDALFTD LVTACVPPSP VDVTKLGSEA
     QEMREGLIRL CSEAEGKLEA HYSDMLAAFD NPLDHLGMFP YYSNYINLSK LEYELLARYV
     PGRHRPARVA FIGSGPLPFS SYVLAARHLP DAMFDNYDLC SAANDRASKL FRADKDVGAR
     MSFHTADVAD LTGELAAYDV VFLAALVGMA AEDKTKVIAH LGAHMADGAA LVVRSAHGHV
     GFLYPIVDPQ DIGRGGFEVL AVCHPDDDVV NSVIIAHKSK DVHANERPNG VVDSTRGAVP
     VVSPPCRFGE MVADVTHKRE EFTNAEVAF