1A15_ORYSJ
ID 1A15_ORYSJ Reviewed; 533 AA.
AC A0A0P0UZP7; O24220; Q9FU17;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 5 {ECO:0000303|PubMed:17012402};
DE Short=ACC synthase 5 {ECO:0000303|PubMed:17012402};
DE Short=OsACS5 {ECO:0000303|PubMed:17012402};
DE EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
GN Name=ACS5 {ECO:0000303|PubMed:17012402}; Synonyms=ACC5 {ECO:0000305};
GN OrderedLocusNames=Os01g0192900 {ECO:0000312|EMBL:BAS70840.1},
GN LOC_Os01g09700 {ECO:0000305};
GN ORFNames=P0671B11.29 {ECO:0000312|EMBL:BAB12704.1};
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION BY SUBMERGENCE.
RX PubMed=12011339; DOI=10.1104/pp.001206;
RA Zhou Z., de Almeida Engler J., Rouan D., Michiels F., Van Montagu M.,
RA Van Der Straeten D.;
RT "Tissue localization of a submergence-induced 1-aminocyclopropane-1-
RT carboxylic acid synthase in rice.";
RL Plant Physiol. 129:72-84(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP 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 [7]
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 shoots and leaf blades
CC (PubMed:30810167). Expressed at low levels in leaf sheaths
CC (PubMed:30810167). Expressed in vasculature of roots and shoots
CC (PubMed:12011339). {ECO:0000269|PubMed:12011339,
CC ECO:0000269|PubMed:30810167}.
CC -!- DEVELOPMENTAL STAGE: During germination and leaf development, expressed
CC in the new developing organs. {ECO:0000269|PubMed:12011339}.
CC -!- INDUCTION: Induced by submergence. {ECO:0000269|PubMed:12011339}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB12704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF04193.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA65776.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97066; CAA65776.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP002746; BAB12704.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008207; BAF04193.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014957; BAS70840.1; -; Genomic_DNA.
DR PIR; T03414; T03414.
DR AlphaFoldDB; A0A0P0UZP7; -.
DR SMR; A0A0P0UZP7; -.
DR STRING; 4530.OS01T0192900-00; -.
DR PaxDb; A0A0P0UZP7; -.
DR EnsemblPlants; Os01t0192900-00; Os01t0192900-00; Os01g0192900.
DR Gramene; Os01t0192900-00; Os01t0192900-00; Os01g0192900.
DR KEGG; osa:4327307; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; A0A0P0UZP7; -.
DR OMA; HRISRFM; -.
DR OrthoDB; 1156861at2759; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
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..533
FT /note="1-aminocyclopropane-1-carboxylate synthase 5"
FT /id="PRO_0000455672"
FT MOD_RES 358
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P37821"
FT CONFLICT 94
FT /note="A -> S (in Ref. 1; CAA65776)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> S (in Ref. 1; CAA65776)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="D -> G (in Ref. 1; CAA65776)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="A -> V (in Ref. 1; CAA65776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 58164 MW; 3D881D96A2479F5A CRC64;
MIMSGFHIGI YTSICLYIPL PHLEPWIISS HTPKNLNLLD CLLYCSVASY TAIAYKFCTA
RLIQSERTRE NIMGGKLLPA AAFAGSAPPL SQVATSAAHG EDSPYFAGWK AYDEDPYHAV
DNPDGVIQMG LAENQVSFDL LEAYLRDHPE AAGWSTGGAG AGSFRDNALF QDYHGLKSFR
KAMASFMGKI RGGKARFDPD HIVLTAGATA ANELLTFILA NPGDALLIPT PYYPGFDRDL
RWRTGVNIVP VRCDSANGFQ VTVAALQAAY DEAAAVGMRA RAVLITNPSN PLGTTVRRKM
LDDILDFVSR NDIHLISDEI YSGSVFAAPD LVSVAELVEA RGGDGIAGRV HIVYSLSKDL
GLPGFRVGVV YSYNDAVVTA ARRMSSFTLV SSQTQKTLAA MLSDEAFAGE YIRTNRRRLR
ERHEHVVAGL ARAGVPCLRG NAGLFVWMDM RRLLLGGGGV GGELRLWEKL LRQAKLNISP
GSSCHCSEAG WFRVCFANMS LDTLDLALHR ISRFMDTWNG TKQQASCQQQ EQQ
