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1A14_ORYSJ
ID   1A14_ORYSJ              Reviewed;         496 AA.
AC   Q5W6F9; A0A0P0WKX8;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 4 {ECO:0000303|PubMed:17012402};
DE            Short=ACC synthase 4 {ECO:0000303|PubMed:17012402};
DE            Short=OsACS4 {ECO:0000303|PubMed:17012402};
DE            EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
GN   Name=ACS4 {ECO:0000303|PubMed:17012402}; Synonyms=ACC4 {ECO:0000305};
GN   OrderedLocusNames=Os05g0319200 {ECO:0000312|EMBL:BAS93346.1},
GN   LOC_Os05g25490 {ECO:0000305};
GN   ORFNames=OSJNBb0006B22.3 {ECO:0000312|EMBL:AAV44081.1},
GN   OSJNBb0059K16.10 {ECO:0000312|EMBL:AAV44121.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
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=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   [4]
RP   TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=17012402; DOI=10.1104/pp.106.085258;
RA   Iwai T., Miyasaka A., Seo S., Ohashi Y.;
RT   "Contribution of ethylene biosynthesis for resistance to blast fungus
RT   infection in young rice plants.";
RL   Plant Physiol. 142:1202-1215(2006).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=30810167; DOI=10.1093/jxb/erz074;
RA   Lee H.Y., Chen Z., Zhang C., Yoon G.M.;
RT   "Editing of the OsACS locus alters phosphate deficiency-induced adaptive
RT   responses in rice seedlings.";
RL   J. Exp. Bot. 70:1927-1940(2019).
CC   -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC       a direct precursor of ethylene in higher plants.
CC       {ECO:0000250|UniProtKB:P37821}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC         H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC         ChEBI:CHEBI:59789; EC=4.4.1.14;
CC         Evidence={ECO:0000250|UniProtKB:P37821};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P37821};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (PubMed:17012402). Expressed in
CC       shoots and leaf blades (PubMed:30810167). Expressed at low levels in
CC       leaf sheaths (PubMed:30810167). {ECO:0000269|PubMed:17012402,
CC       ECO:0000269|PubMed:30810167}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AC136224; AAV44081.1; -; Genomic_DNA.
DR   EMBL; AC134344; AAV44121.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS93346.1; -; Genomic_DNA.
DR   RefSeq; XP_015638322.1; XM_015782836.1.
DR   AlphaFoldDB; Q5W6F9; -.
DR   SMR; Q5W6F9; -.
DR   STRING; 4530.OS05T0319200-00; -.
DR   PaxDb; Q5W6F9; -.
DR   PRIDE; Q5W6F9; -.
DR   EnsemblPlants; Os05t0319200-00; Os05t0319200-00; Os05g0319200.
DR   GeneID; 107275635; -.
DR   Gramene; Os05t0319200-00; Os05t0319200-00; Os05g0319200.
DR   KEGG; osa:107275635; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   InParanoid; Q5W6F9; -.
DR   OMA; HGIEYAT; -.
DR   OrthoDB; 1156861at2759; -.
DR   PlantReactome; R-OSA-1119334; Ethylene biosynthesis from methionine.
DR   PlantReactome; R-OSA-1119624; Methionine salvage pathway.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   2: Evidence at transcript level;
KW   Ethylene biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..496
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 4"
FT                   /id="PRO_0000455671"
FT   MOD_RES         300
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37821"
SQ   SEQUENCE   496 AA;  53509 MW;  80D3FCB007190273 CRC64;
     MGVKLLADGC AGASSSPALS RVATSAAHGE GSPYFAGWKA YDEDPYDAAA NPDGVIQMGL
     AENQVSIDLL EGYLREHPEA AAWGVAGDGG GDSFRDNALF QDYHGLANFR KAMARFMEKI
     MGGKATFDPD RIVLTAGATA ANELLTFILA DPRDALLIPT PYYPGFDRDL RWRTGVNVVP
     VHCDSANGFQ VTAAALQAAH DEAAAAGMRV RGVLITNPSN PLGTTARREA LEGILGFVAR
     NDIHLVSDEI YSGSVFAAPD LVSVAELVES SSSRARHRGE DDDGDVGVAD RVHVVYSLSK
     DLGLPGFRVG VVYSRNDAVV AAARRMSSFT LVSSQTQRTL AAVLSDEAFV DAYVAANRAR
     LRERHDHVVA GLARAGVPCL RGNAGLFVWM DMRRLLLGDG GDAATFAGEL RLWDRLLREV
     KLNVSPGSSC HCSEPGWFRV CFANMSLATL DVALERISRF MDAWCKATIG KFNHLQPNRC
     EVNYFALERY QGHVQQ
 
 
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