ID 1A14_ARATH Reviewed; 474 AA. AC Q43309; Q9S9C4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 60. DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 4; DE Short=ACC synthase 4; DE EC=4.4.1.14; DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 4; GN Name=ACS4; Synonyms=ACC4; OrderedLocusNames=At2g22810; GN ORFNames=T20K9.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND RP INDUCTION. RC STRAIN=cv. Columbia; RX MEDLINE=95370228; PubMed=7642574; DOI=10.1074/jbc.270.32.19093; RA Abel S., Nguyen M.D., Chow W., Theologis A.; RT "ACS4, a primary indoleacetic acid-responsive gene encoding 1- RT aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana. RT Structural characterization, expression in Escherichia coli, and RT expression characteristics in response to auxin."; RL J. Biol. Chem. 270:19093-19099(1995). RN [2] RP ERRATUM. RA Abel S., Nguyen M.D., Chow W., Theologis A.; RL J. Biol. Chem. 270:26020-26020(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE OF 50-81. RX MEDLINE=93066381; PubMed=1438312; DOI=10.1073/pnas.89.22.11046; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [6] RP ENZYME ACTIVITY, AND INDUCTION. RX PubMed=12968022; DOI=10.1074/jbc.M308297200; RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., RA Theologis A.; RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate RT synthase isozymes encoded by the Arabidopsis gene family."; RL J. Biol. Chem. 278:49102-49112(2003). CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of CC ethylene. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane- CC 1-carboxylate + methylthioadenosine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 uM for AdoMet; CC Vmax=31.20 uM/h/mg enzyme; CC pH dependence: CC Optimum pH is 7.8; CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S- CC adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step CC 1/2. CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of CC heterodimerization with other ACS enzymes is however unsure (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers. CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). CC By auxin. CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation CC of such stability, play a central role in ethylene biosynthesis. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U23481; AAC49037.1; -; mRNA. DR EMBL; U23482; AAA85039.1; -; Genomic_DNA. DR EMBL; AC004786; AAC32428.1; -; Genomic_DNA. DR EMBL; AC005617; AAM15065.1; -; Genomic_DNA. DR EMBL; AF332404; AAG48767.1; -; mRNA. DR IPI; IPI00519589; -. DR PIR; B84617; B84617. DR PIR; G46376; G46376. DR RefSeq; NP_179866.1; -. DR UniGene; At.1549; -. DR HSSP; P37821; 1B8G. DR SMR; Q43309; 10-431. DR GeneID; 816812; -. DR GenomeReviews; CT485783_GR; AT2G22810. DR KEGG; ath:AT2G22810; -. DR NMPDR; fig|3702.1.peg.9299; -. DR GeneFarm; 4050; -. DR TAIR; At2g22810; -. DR OMA; Q43309; TELLEFF. DR BRENDA; 4.4.1.14; 302. DR ArrayExpress; Q43309; -. DR GermOnline; AT2G22810; Arabidopsis thaliana. DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IDA:TAIR. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0016769; F:transferase activity, transferring nitrogen...; IEA:InterPro. DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009835; P:ripening; IEA:UniProtKB-KW. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR004839; Aminotrans_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Ethylene biosynthesis; Fruit ripening; Lyase; KW Pyridoxal phosphate; S-adenosyl-L-methionine. FT CHAIN 1 474 1-aminocyclopropane-1-carboxylate FT synthase 4. FT /FTId=PRO_0000123898. FT BINDING 47 47 Substrate (By similarity). FT BINDING 85 85 Substrate (By similarity). FT MOD_RES 273 273 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 474 AA; 53795 MW; 98FD27622EAF3C21 CRC64; MVQLSRKATC NSHGQVSSYF LGWEEYEKNP YDVTKNPQGI IQMGLAENQL CFDLLESWLA QNTDAACFKR DGQSVFRELA LFQDYHGLSS FKNAFADFMS ENRGNRVSFD SNNLVLTAGA TSANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGVEI VPIQSSSTNG FRITKLALEE AYEQAKKLDL NVKGILITNP SNPLGTTTTQ TELNILFDFI TKNKNIHLVS DEIYSGTVFN SSEFISVMEI LKNNQLENTD VLNRVHIVCS LSKDLGLPGF RVGAIYSNDK DVISAATKMS SFGLVSSQTQ YLLSSLLSDK KFTKNYLREN QKRLKNRQRK LVLGLEAIGI KCLKSNAGLF CWVDMRPLLR SKTFEAEMDL WKKIVYEVKL NISPGSSCHC EEPGWFRVCF ANMIDETLKL ALKRLKMLVD DENSSRRCQK SKSERLNGSR KKTMSNVSNW VFRLSFHDRE AEER //