(data stored in SCRATCH zone)

SWISSPROT: D3VH73_XENNA

ID   D3VH73_XENNA            Unreviewed;       403 AA.
AC   D3VH73;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
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=XNC1_0270 {ECO:0000313|EMBL:CBJ88358.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88358.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88358.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88358.1; -; Genomic_DNA.
DR   RefSeq; WP_013183207.1; NC_014228.1.
DR   STRING; 406817.XNC1_0270; -.
DR   EnsemblBacteria; CBJ88358; CBJ88358; XNC1_0270.
DR   KEGG; xne:XNC1_0270; -.
DR   eggNOG; ENOG4105CDH; Bacteria.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; PAREWGM; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000008075; Chromosome.
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; D3VH73.
DR   SWISS-2DPAGE; D3VH73.
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:UP000008075};
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:CBJ88358.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00693589};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   NP_BIND      11     19       ATP. {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING      39     39       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING      91     91       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING      96     96       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     121    121       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING     123    123       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     127    127       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     127    127       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     128    128       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     131    131       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     180    180       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     189    189       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     265    265       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     277    277       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
SQ   SEQUENCE   403 AA;  44709 MW;  778F82CDCC7271C9 CRC64;
     MTKSIKKIVL AYSGGLDTSA IIPWLKEHYD DCEVIAFVAD VGQSREDLEG VEQKALSSGA
     SECHVVDLRE VFIKEYVYPV LKTGALYEGS YLLGTSMARP IIAKAQVELA LKVGADAVAH
     GATGKGNDQV RFESTYTALV PHLKVVAPWR EWDLCSREAL LDYLKVRDIP TTATLEKIYS
     RDENAWHIST EGGVLESTWN AANKDCWAWT TEPEDAPNEP EYVTVTVEKG EVIGVNGQVL
     SPYQCLNALN ELGAKHGIGR IDIVENRLVG MKSRGCYETP GGTIMMEALR GIEQLVLDRD
     SFKWRQQLGL EMSYVVYDGR WFAPLRQSIQ AAAETLAASV SGEVILKLYK GQVTAVQKKS
     THSLYSEEFA TFGEDEVYDH SHAEGFIRLY SLSSRIRALN SKK
//

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