(data stored in SCRATCH zone)

SWISSPROT: C1E0R8_MICCC

ID   C1E0R8_MICCC            Unreviewed;       424 AA.
AC   C1E0R8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Adenylosuccinate synthetase, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03125};
DE            Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125};
DE            Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125};
DE            EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125};
GN   Name=PURA {ECO:0000256|HAMAP-Rule:MF_03125};
GN   ORFNames=MICPUN_97107 {ECO:0000313|EMBL:ACO61604.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61604.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61604.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- FUNCTION: Plays an important role in the de novo pathway and in
CC       the salvage pathway of purine nucleotide biosynthesis. Catalyzes
CC       the first commited step in the biosynthesis of AMP from IMP.
CC       {ECO:0000256|HAMAP-Rule:MF_03125}.
CC   -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03125};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03125};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_03125}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03125}.
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DR   EMBL; CP001324; ACO61604.1; -; Genomic_DNA.
DR   RefSeq; XP_002500346.1; XM_002500300.1.
DR   GeneID; 8241981; -.
DR   KEGG; mis:MICPUN_97107; -.
DR   HOGENOM; HOG000260959; -.
DR   InParanoid; C1E0R8; -.
DR   KO; K01939; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11846; PTHR11846; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 1.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00184; purA; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E0R8.
DR   SWISS-2DPAGE; C1E0R8.
KW   Chloroplast {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   NP_BIND      12     18       GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   NP_BIND      40     42       GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   NP_BIND     329    331       GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   NP_BIND     412    414       GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   REGION       13     16       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_03125}.
FT   REGION       38     41       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_03125}.
FT   REGION      297    303       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03125}.
FT   ACT_SITE     13     13       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03125}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03125}.
FT   ACT_SITE    142    142       {ECO:0000256|PROSITE-ProRule:PRU10134}.
FT   METAL        13     13       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03125}.
FT   METAL        40     40       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     131    131       IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     145    145       IMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     222    222       IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     237    237       IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     301    301       IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
FT   BINDING     303    303       GTP. {ECO:0000256|HAMAP-Rule:MF_03125}.
SQ   SEQUENCE   424 AA;  46011 MW;  883ADFEC0BAD2D82 CRC64;
     MSAVALSSAA WGDEGKGKLV DILAQEYDIV ARCQGGANAG HTIYDDEGKK YALHLVPSGI
     LNEKAKCVVG NGVVVHLPGM FNEIDTLEKA GVKIDASRLV ISDRAHMLFD LHKEIDGLRE
     AELSGNKIGT TKRGIGPAYA SKATRNGIRV GDIRNPETFA QKLRTLAADA AARFEDFEYD
     VEAELVAYQK YAERITPFIA DTVHMINEEH KAGKRVLVEG ANATMLDLDF GTYPFVTSSN
     PSLGGVCSGL GLAPNKFETV IGVAKAYTTR VGAGPYPTEL FGELADDLRE KGYEYGTTTG
     RPRRIGWLDV VALNYASAIN GFTHLNLTKL DVLSGLPELK IATAYKLGDG TVTNAFPSSI
     EELEKVECVY ETLPGWEEDI SKMRDWDELP AKCKAYVEKI EELTGVECRY LGVGPGRDAI
     VVKP
//

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