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Database: UniProt
Entry: P24532
LinkDB: P24532
Original site: P24532 
ID   ASSY_STRCO              Reviewed;         481 AA.
AC   P24532; Q9FC47;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   29-OCT-2014, entry version 119.
DE   RecName: Full=Argininosuccinate synthase;
DE            EC=6.3.4.5;
DE   AltName: Full=Citrulline--aspartate ligase;
GN   Name=argG; OrderedLocusNames=SCO7036; ORFNames=SC4G1.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces;
OC   Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Ishihara H., Urabe H., Kasama H., Ogawara H.;
RT   "Nucleotide sequence of the gene encoding argininosuccinate synthetase
RT   in Streptomyces coelicolor A3(2).";
RL   Nihon Hosenkin Gakkaishi 5:14-17(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       2 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA00691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D00799; BAA00691.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL939130; CAC01534.1; -; Genomic_DNA.
DR   PIR; JQ1057; AJSMRC.
DR   RefSeq; NP_631098.1; NC_003888.3.
DR   ProteinModelPortal; P24532; -.
DR   SMR; P24532; 2-432.
DR   STRING; 100226.SCO7036; -.
DR   PRIDE; P24532; -.
DR   EnsemblBacteria; CAC01534; CAC01534; CAC01534.
DR   GeneID; 1102474; -.
DR   KEGG; sco:SCO7036; -.
DR   PATRIC; 23743995; VBIStrCoe124346_7140.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230094; -.
DR   InParanoid; P24532; -.
DR   KO; K01940; -.
DR   OMA; RQEMSEF; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   PhylomeDB; P24532; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.287.400; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.1260.10; -; 1.
DR   HAMAP; MF_00581; Arg_succ_synth_type2; 1.
DR   InterPro; IPR023437; Arg_succ_synth_type2_subfam.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR024074; AS_cat/multimer_dom_body.
DR   InterPro; IPR024073; AS_multimer_C_tail.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    481       Argininosuccinate synthase.
FT                                /FTId=PRO_0000148708.
FT   NP_BIND      17     25       ATP. {ECO:0000250}.
FT   BINDING      43     43       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING      99     99       Citrulline. {ECO:0000250}.
FT   BINDING     129    129       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING     131    131       Aspartate. {ECO:0000250}.
FT   BINDING     131    131       ATP. {ECO:0000250}.
FT   BINDING     135    135       Aspartate. {ECO:0000250}.
FT   BINDING     135    135       Citrulline. {ECO:0000250}.
FT   BINDING     136    136       Aspartate. {ECO:0000250}.
FT   BINDING     136    136       ATP. {ECO:0000250}.
FT   BINDING     139    139       Citrulline. {ECO:0000250}.
FT   BINDING     192    192       Citrulline. {ECO:0000250}.
FT   BINDING     194    194       ATP. {ECO:0000250}.
FT   BINDING     201    201       Citrulline. {ECO:0000250}.
FT   BINDING     203    203       Citrulline. {ECO:0000250}.
FT   BINDING     280    280       Citrulline. {ECO:0000250}.
FT   CONFLICT     75     83       AALVEEGLA -> RRWSRRGWG (in Ref. 1;
FT                                BAA00691). {ECO:0000305}.
FT   CONFLICT    181    181       L -> F (in Ref. 1; BAA00691).
FT                                {ECO:0000305}.
FT   CONFLICT    265    272       NAVGGRHG -> TPSAAGTA (in Ref. 1;
FT                                BAA00691). {ECO:0000305}.
FT   CONFLICT    326    326       R -> P (in Ref. 1; BAA00691).
FT                                {ECO:0000305}.
FT   CONFLICT    426    428       LGL -> SRF (in Ref. 1; BAA00691).
FT                                {ECO:0000305}.
FT   CONFLICT    435    435       A -> P (in Ref. 1; BAA00691).
FT                                {ECO:0000305}.
SQ   SEQUENCE   481 AA;  52270 MW;  18E7DE4BEABF98B3 CRC64;
     MSKVLTSLPT GERVGIAFSG GLDTSVAVAW MRDKGAVPCT YTADIGQYDE PDIASVPDRA
     KTYGAEVARL VDCRAALVEE GLAALTCGAF HIRSGGRAYF NTTPLGRAVT GTLLVRAMLE
     DDVQIWGDGS TFKGNDIERF YRYGLLANPQ LRIYKPWLDA DFVTELGGRK EMSEWLVAHD
     LPYRDSTEKA YSTDANIWGA THEAKTLEHL DTGVETVEPI MGVRFWDPSV EIAPEDVTIG
     FDQGRPVTIN GKEFASAVDL VMEANAVGGR HGMGMSDQIE NRIIEAKSRG IYEAPGMALL
     HAAYERLVNA IHNEDTLAQY HTEGRRLGRL MYEGRWLDPQ SLMIRESLQR WVGSAVTGEV
     TLRLRRGEDY SILDTTGPAF SYHPDKLSME RTEDSAFGPV DRIGQLTMRN LDIADSRAKL
     EQYAGLGLIG TANPAIGAAQ AAATGLIGAM PEGGAQAIAS RGEVSADDEL LDRAAMESGT
     D
//
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