Entry euk:ASSY_ARATH

ID   ASSY_ARATH              Reviewed;         494 AA.
AC   Q9SZX3; Q8VZ47;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 3.
DT   12-APR-2017, entry version 140.
DE   RecName: Full=Argininosuccinate synthase, chloroplastic;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g24830; ORFNames=F6I7.40;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   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   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-74, CLEAVAGE OF TRANSIT
RP   PEPTIDE [LARGE SCALE ANALYSIS] AFTER ARG-73, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + N(omega)-(L-arginino)succinate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SZX3-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB41123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049657; CAB41123.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161562; CAB79393.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84968.1; -; Genomic_DNA.
DR   EMBL; AY065252; AAL38728.1; -; mRNA.
DR   EMBL; AY091319; AAM14258.1; -; mRNA.
DR   PIR; T06667; T06667.
DR   RefSeq; NP_194214.2; NM_118616.5. [Q9SZX3-1]
DR   UniGene; At.3133; -.
DR   ProteinModelPortal; Q9SZX3; -.
DR   SMR; Q9SZX3; -.
DR   BioGrid; 13875; 1.
DR   STRING; 3702.AT4G24830.1; -.
DR   SwissPalm; Q9SZX3; -.
DR   PaxDb; Q9SZX3; -.
DR   PRIDE; Q9SZX3; -.
DR   EnsemblPlants; AT4G24830.1; AT4G24830.1; AT4G24830. [Q9SZX3-1]
DR   GeneID; 828586; -.
DR   Gramene; AT4G24830.1; AT4G24830.1; AT4G24830.
DR   KEGG; ath:AT4G24830; -.
DR   Araport; AT4G24830; -.
DR   TAIR; locus:2126803; AT4G24830.
DR   eggNOG; KOG1706; Eukaryota.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   InParanoid; Q9SZX3; -.
DR   KO; K01940; -.
DR   OMA; DPANEPM; -.
DR   OrthoDB; EOG093607A2; -.
DR   PhylomeDB; Q9SZX3; -.
DR   BioCyc; ARA:AT4G24830-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   PRO; PR:Q9SZX3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZX3; baseline and differential.
DR   Genevisible; Q9SZX3; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IBA:GO_Central.
DR   CDD; cd01999; Argininosuccinate_Synthase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.1260.10; -; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR   InterPro; IPR024074; AS_cat/multimer_dom_body.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11587; PTHR11587; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   TIGRFAMs; TIGR00032; argG; 1.
DR   PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW   Arginine biosynthesis; ATP-binding; Chloroplast; Complete proteome;
KW   Ligase; Nucleotide-binding; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     73       Chloroplast.
FT                                {ECO:0000244|PubMed:22223895,
FT                                ECO:0000255}.
FT   CHAIN        74    494       Argininosuccinate synthase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000002412.
FT   NP_BIND     102    110       ATP. {ECO:0000250}.
FT   BINDING     129    129       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     181    181       Citrulline. {ECO:0000250}.
FT   BINDING     186    186       Citrulline. {ECO:0000250}.
FT   BINDING     211    211       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING     213    213       Aspartate. {ECO:0000250}.
FT   BINDING     217    217       Aspartate. {ECO:0000250}.
FT   BINDING     217    217       Citrulline. {ECO:0000250}.
FT   BINDING     218    218       Aspartate. {ECO:0000250}.
FT   BINDING     221    221       Citrulline. {ECO:0000250}.
FT   BINDING     270    270       Citrulline. {ECO:0000250}.
FT   BINDING     279    279       Citrulline. {ECO:0000250}.
FT   BINDING     355    355       Citrulline. {ECO:0000250}.
FT   BINDING     367    367       Citrulline. {ECO:0000250}.
FT   MOD_RES      74     74       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       100    486       ipfam:Arginosuc_synth [T]
FT   MYHIT        96    492       ihamap:Arg_succ_synth_type1 [T]
FT   MYHIT       211    222       ipat:ARGININOSUCCIN_SYN_2 [T]
FT   MYHIT       102    110       ipat:ARGININOSUCCIN_SYN_1 [T]
SQ   SEQUENCE   494 AA;  53846 MW;  926F8D01AF32F052 CRC64;
     MAEISATSFP SSSSSALVIR SSHNGSLKCQ NVAVPKTTSQ FQELSLKRSQ LVGNAVVTGH
     VTGSRSCKNQ AIRAVLSGDG TALTTDSKEA GLRGKLKKVV LAYSGGLDTS VIVPWLKENY
     GCEVVCFTAD VGQGIKELEG LEQKAKASGA SQLVVKDLTE EFVKDFIFPC LRAGAIYERK
     YLLGTSMARP VIAKAMVDVA AEVGADAVAH GCTGKGNDQV RFELTFFSLN PELKVVAPWR
     EWEIQGREDA IEYAKKHNVP VPVTKKSIYS RDRNLWHLSH EGDLLEDPAN EPKKDMYMMS
     VDPEDAPDQP EYIEIGIESG LPVALNGKAL SPATLLAELN TIGGKHGIGR IDMVENRLVG
     MKSRGVYETP GGTILFAAVQ ELESLTLDRE SIQVKDTLAL KYAEMVYAGR WFDPLRESMD
     AFMEKITETT TGSVTLKLYK GSVSVTGRQS PNSLYRQDIS SFEGSEIYNQ ADAAGFIRLY
     GLPMKIRAML KKIS
//