ASSY_STRCO
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 03-AUG-2022, entry version 153.
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; Streptomycetales; Streptomycetaceae;
OC Streptomyces; 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 in
RT 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., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:456215; EC=6.3.4.5;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC 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 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 RefSeq; WP_003972108.1; NZ_VNID01000012.1.
DR AlphaFoldDB; P24532; -.
DR SMR; P24532; -.
DR STRING; 100226.SCO7036; -.
DR PRIDE; P24532; -.
DR GeneID; 1102474; -.
DR KEGG; sco:SCO7036; -.
DR PATRIC; fig|100226.15.peg.7140; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_1_11; -.
DR InParanoid; P24532; -.
DR OMA; GRAYFNT; -.
DR PhylomeDB; P24532; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IBA:GO_Central.
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 SUPFAM; SSF69864; SSF69864; 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; Cytoplasm;
KW Ligase; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..481
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148708"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250"
FT CONFLICT 75..83
FT /note="AALVEEGLA -> RRWSRRGWG (in Ref. 1; BAA00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="L -> F (in Ref. 1; BAA00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..272
FT /note="NAVGGRHG -> TPSAAGTA (in Ref. 1; BAA00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="R -> P (in Ref. 1; BAA00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 426..428
FT /note="LGL -> SRF (in Ref. 1; BAA00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="A -> P (in Ref. 1; BAA00691)"
FT /evidence="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
