(data stored in SCRATCH zone)

SWISSPROT: D5US91_TSUPD

ID   D5US91_TSUPD            Unreviewed;       428 AA.
AC   D5US91;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE            Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
DE            Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000256|HAMAP-Rule:MF_00011};
GN   OrderedLocusNames=Tpau_0517 {ECO:0000313|EMBL:ADG77158.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77158.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77158.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis. Catalyzes the first committed step in the
CC       biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC         dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
CC       ECO:0000256|RuleBase:RU000520}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
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DR   EMBL; CP001966; ADG77158.1; -; Genomic_DNA.
DR   RefSeq; WP_013125200.1; NC_014158.1.
DR   STRING; 521096.Tpau_0517; -.
DR   EnsemblBacteria; ADG77158; ADG77158; Tpau_0517.
DR   KEGG; tpr:Tpau_0517; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   OrthoDB; 232152at2; -.
DR   BioCyc; TPAU521096:G1GKO-500-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   Gene3D; 1.10.300.10; -; 1.
DR   Gene3D; 3.40.440.10; -; 1.
DR   Gene3D; 3.90.170.10; -; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR   InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR   InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR   InterPro; IPR042111; Adenylosuccinate_synth_dom3.
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; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5US91.
DR   SWISS-2DPAGE; D5US91.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520, ECO:0000313|EMBL:ADG77158.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213}.
FT   NP_BIND      12     18       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND      40     42       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     331    333       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     413    415       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   REGION       13     16       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION       38     41       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION      299    305       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00011}.
FT   COILED      194    214       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     13     13       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE    140    140       {ECO:0000256|PROSITE-ProRule:PRU10134}.
FT   METAL        13     13       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   METAL        40     40       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     129    129       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     143    143       IMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     224    224       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     239    239       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     303    303       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     305    305       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   428 AA;  46670 MW;  0597AD353B69C1DC CRC64;
     MPAIVLIGAQ WGDEGKGKAT DLLGEKLQWV VRYQGGNNAG HTVVLPNGDK FALHLIPSGI
     LTPGVKNVIG NGVVVDPSVL LQELDGLEAR GVDTSNLLLS ADAHLLMPYH VAIDKVTERF
     LGNKKIGTTG RGIGPCYQDK IARVGVRAQD VLDESILTQK VEAALEFKNQ VLTKIYNRRA
     LDPRQVVDET LELAESFKHR IADTRLELNK ALERGETVLL EGSQGTLLDV DHGTYPFVTS
     SNPTSGGASV GSGIGPTRIT TVLGILKAYT TRVGSGPFPT ELFDEWGEYL AKHGGEVGVT
     TGRARRCGWF DAVIARYATR VNGITDYFLT KLDVLSSIEN VPICVAYEID GVRYDEMPTT
     QSQVHHATPI FETMPGWWED ISECRTFEEL PKNAQNYVLR LEELSGAHIS CIGVGPGRDE
     TIVRRPIV
//

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