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NAAT1_ORYSJ
ID   NAAT1_ORYSJ             Reviewed;         494 AA.
AC   A0A0P0VI36; A9CM06; C7IYK7; Q6K2Y8;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Nicotianamine aminotransferase 1 {ECO:0000303|PubMed:15781441};
DE            Short=OsNAAT1 {ECO:0000303|PubMed:15781441};
DE            EC=2.6.1.80 {ECO:0000269|PubMed:18034312};
GN   Name=NAAT1 {ECO:0000303|PubMed:15781441};
GN   OrderedLocusNames=Os02g0306401 {ECO:0000312|EMBL:BAS78288.1},
GN   LOC_Os02g20360 {ECO:0000305};
GN   ORFNames=P0543C11.29 {ECO:0000312|EMBL:BAD23582.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RA   Nishizawa N.K., Takahashi M., Suzuki M., Nakanishi H., Satoshi M.,
RA   Yoshimura E.;
RT   "Phytosiderophore secretion in zinc-deficient barley is independent of iron
RT   deficiency.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 35-494.
RX   PubMed=16972867; DOI=10.1111/j.1365-313x.2006.02853.x;
RA   Suzuki M., Takahashi M., Tsukamoto T., Watanabe S., Matsuhashi S.,
RA   Yazaki J., Kishimoto N., Kikuchi S., Nakanishi H., Mori S., Nishizawa N.K.;
RT   "Biosynthesis and secretion of mugineic acid family phytosiderophores in
RT   zinc-deficient barley.";
RL   Plant J. 48:85-97(2006).
RN   [6]
RP   INDUCTION BY IRON DEFICIENCY.
RX   PubMed=15781441; DOI=10.1093/jxb/eri131;
RA   Kobayashi T., Suzuki M., Inoue H., Itai R.N., Takahashi M., Nakanishi H.,
RA   Mori S., Nishizawa N.K.;
RT   "Expression of iron-acquisition-related genes in iron-deficient rice is co-
RT   ordinately induced by partially conserved iron-deficiency-responsive
RT   elements.";
RL   J. Exp. Bot. 56:1305-1316(2005).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17333504; DOI=10.1007/s11103-007-9132-4;
RA   Nozoye T., Inoue H., Takahashi M., Ishimaru Y., Nakanishi H., Mori S.,
RA   Nishizawa N.K.;
RT   "The expression of iron homeostasis-related genes during rice
RT   germination.";
RL   Plant Mol. Biol. 64:35-47(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY IRON
RP   DEFICIENCY.
RX   PubMed=18034312; DOI=10.1007/s11103-007-9262-8;
RA   Inoue H., Takahashi M., Kobayashi T., Suzuki M., Nakanishi H., Mori S.,
RA   Nishizawa N.K.;
RT   "Identification and localisation of the rice nicotianamine aminotransferase
RT   gene OsNAAT1 expression suggests the site of phytosiderophore synthesis in
RT   rice.";
RL   Plant Mol. Biol. 66:193-203(2008).
CC   -!- FUNCTION: Involved in biosynthesis of mugineic acid family
CC       phytosiderophores, which are ferric iron chelators produced in
CC       graminaceous plants in response to iron deficiency.
CC       {ECO:0000269|PubMed:18034312}.
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:18034312};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P17735};
CC   -!- TISSUE SPECIFICITY: Expressed in companion and pericycle cells adjacent
CC       to the protoxylem of roots (PubMed:18034312). Expressed in companion
CC       cells of shoots (PubMed:18034312). {ECO:0000269|PubMed:18034312}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the scutellum and leaf primordium of
CC       fully mature seeds (PubMed:17333504). In germinating seeds, expressed
CC       in the vascular bundle of the scutellum, the coleoptile, the bud scale,
CC       the coleorhiza, and the base of the seminal root (PubMed:17333504).
CC       {ECO:0000269|PubMed:17333504}.
CC   -!- INDUCTION: Induced by iron deficiency in roots and leaves.
CC       {ECO:0000269|PubMed:15781441, ECO:0000269|PubMed:18034312}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD23582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE86873.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAH91645.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB182275; BAF95202.1; -; mRNA.
DR   EMBL; AP005743; BAD23582.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008208; BAH91645.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; BAS78288.1; -; Genomic_DNA.
DR   EMBL; AB206814; BAE86873.1; ALT_INIT; mRNA.
DR   RefSeq; XP_015627400.1; XM_015771914.1.
DR   AlphaFoldDB; A0A0P0VI36; -.
DR   SMR; A0A0P0VI36; -.
DR   STRING; 4530.OS02T0306401-00; -.
DR   PaxDb; A0A0P0VI36; -.
DR   EnsemblPlants; Os02t0306401-00; Os02t0306401-00; Os02g0306401.
DR   GeneID; 9267778; -.
DR   Gramene; Os02t0306401-00; Os02t0306401-00; Os02g0306401.
DR   KEGG; osa:9267778; -.
DR   eggNOG; KOG0259; Eukaryota.
DR   HOGENOM; CLU_017584_4_2_1; -.
DR   OMA; GYCQAVL; -.
DR   OrthoDB; 734452at2759; -.
DR   BRENDA; 2.6.1.80; 4460.
DR   PlantReactome; R-OSA-9025754; Mugineic acid biosynthesis.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0033855; F:nicotianamine aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
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; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..494
FT                   /note="Nicotianamine aminotransferase 1"
FT                   /id="PRO_0000446970"
FT   REGION          24..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P17735"
FT   CONFLICT        38
FT                   /note="S -> F (in Ref. 1; BAF95202)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  53822 MW;  783C28C759FF1FAF CRC64;
     MHASCCCAPP ESVSHTRRIS YKYSGTSYPT RTTTTSSSAP EFTNKKQSTA MAPTTAAAAA
     SSNGGGESDG SSKEWRLTAP TRGGAMAAAG DKMSIRAVRY KISASVDDRG PRPVLPLAHG
     DPSVFPEFRT AAEAEDAVAD ALRSGDFNCY PAGVGLPAAR RAVADHLSRD LPYKLSSDDI
     FLTAGGTQAI EVVISILAQP GTNILLPRPG YPNYEARAAF NNLEVRHFDL IPEKGWEIDL
     NSLESIADKN TTAIVIINPN NPCGNVYTYE HLSKVAEVAR KLGILVITDE VYGNLVFGSS
     PFVPMGCFGH IVPILTIGSL SKRWIVPGWR LGWVAICDPK KTLQETKIAT LITNFLNVST
     DPATFIQGAL PNILKNTKEE FFKRIIDLLT ETSDICYRGI KDIKCITCPH KPEGSMFVMV
     KLNLYLLEGI HDDVDFCCQL AKEESVILCP GSVLGMKNWV RITFAIDSSS LLDGLERIKS
     FCQRHKKKNP LNYI
 
 
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