(data stored in SCRATCH zone)

SWISSPROT: D1CE90_THET1

ID   D1CE90_THET1            Unreviewed;       403 AA.
AC   D1CE90;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00693586};
DE            EC=6.3.4.5 {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00693595};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00005};
GN   Name=argG {ECO:0000256|HAMAP-Rule:MF_00005};
GN   OrderedLocusNames=Tter_0324 {ECO:0000313|EMBL:ACZ41246.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41246.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41246.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC         arginino)succinate + AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472,
CC         ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00005,
CC         ECO:0000256|SAAS:SAAS01117911};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00693596}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00693599}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00693601}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00693593}.
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DR   EMBL; CP001825; ACZ41246.1; -; Genomic_DNA.
DR   RefSeq; WP_012874281.1; NC_013525.1.
DR   STRING; 525904.Tter_0324; -.
DR   EnsemblBacteria; ACZ41246; ACZ41246; Tter_0324.
DR   KEGG; ttr:Tter_0324; -.
DR   eggNOG; ENOG4105CDH; Bacteria.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; PAREWGM; -.
DR   OrthoDB; 357142at2; -.
DR   BioCyc; TTER525904:G1GGS-328-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; D1CE90.
DR   SWISS-2DPAGE; D1CE90.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693590};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693591};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693602};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693598};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693592, ECO:0000313|EMBL:ACZ41246.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693589};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   NP_BIND      10     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING      37     37       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING      88     88       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING      93     93       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     118    118       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING     120    120       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     124    124       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     124    124       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     125    125       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     128    128       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     177    177       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     186    186       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     262    262       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     274    274       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
SQ   SEQUENCE   403 AA;  45006 MW;  38DD63E6AD8D11B4 CRC64;
     MEKIKKVVLA YSGGLDTSVI LAWIKENYGA EVIAFTADVG QGEEVEEAKQ KALATGASKA
     YALDLREEFV RDFVFPVIRA AAVYENQYLM GTSIARPLIA RELVRIAREE GADAIAHGAT
     GKGNDQVRFE LTAYALQPDI KVIAPWREWS FKGRTDLINY AKEKGIPVPV TPERPYSIDA
     NLFHISYEGG VLEDPWVAPP KGMWRLTRDP EDAPDVPEEI EIEFEAGNPV AVNGQRMGPL
     ELLQCLNQIA GKHGVGRVDI VENRFVGMKS RGCYETPGGT LLHIAHRAVE SITLDREVMH
     LRDQLIPQYA EMVYNGFWYA PERIALQKFM DDIQQRVSGV ARLKLYKGNA YVTGRKSDAS
     LYDHKTVTFE EDEVYNQADA GGFIRLQALR LRTHAAKRLG PGE
//

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