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 01-MAY-2013, entry version 111.
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.
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC 2 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00691.1; Type=Erroneous initiation;
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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 EnsemblBacteria; CAC01534; CAC01534; CAC01534.
DR GeneID; 1102474; -.
DR KEGG; sco:SCO7036; -.
DR PATRIC; 23743995; VBIStrCoe124346_7140.
DR eggNOG; COG0137; -.
DR HOGENOM; HOG000230094; -.
DR KO; K01940; -.
DR OMA; GGRKEMS; -.
DR ProtClustDB; PRK05370; -.
DR UniPathway; UPA00068; UER00113.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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 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;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 481 Argininosuccinate synthase.
FT /FTId=PRO_0000148708.
FT NP_BIND 17 25 ATP (By similarity).
FT BINDING 43 43 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 99 99 Citrulline (By similarity).
FT BINDING 129 129 ATP; via amide nitrogen (By similarity).
FT BINDING 131 131 Aspartate (By similarity).
FT BINDING 131 131 ATP (By similarity).
FT BINDING 135 135 Aspartate (By similarity).
FT BINDING 135 135 Citrulline (By similarity).
FT BINDING 136 136 Aspartate (By similarity).
FT BINDING 136 136 ATP (By similarity).
FT BINDING 139 139 Citrulline (By similarity).
FT BINDING 192 192 Citrulline (By similarity).
FT BINDING 194 194 ATP (By similarity).
FT BINDING 201 201 Citrulline (By similarity).
FT BINDING 203 203 Citrulline (By similarity).
FT BINDING 280 280 Citrulline (By similarity).
FT CONFLICT 75 83 AALVEEGLA -> RRWSRRGWG (in Ref. 1;
FT BAA00691).
FT CONFLICT 181 181 L -> F (in Ref. 1; BAA00691).
FT CONFLICT 265 272 NAVGGRHG -> TPSAAGTA (in Ref. 1;
FT BAA00691).
FT CONFLICT 326 326 R -> P (in Ref. 1; BAA00691).
FT CONFLICT 426 428 LGL -> SRF (in Ref. 1; BAA00691).
FT CONFLICT 435 435 A -> P (in Ref. 1; BAA00691).
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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