ASSY_ECOLI
ID ASSY_ECOLI Reviewed; 447 AA.
AC P0A6E4; P22767; Q2M939;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Argininosuccinate synthase;
DE EC=6.3.4.5;
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=argG; OrderedLocusNames=b3172, JW3140;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=2123815; DOI=10.1016/0378-1119(90)90419-r;
RA van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P.,
RA Nakamura Y., Baumberg S., Glansdorff N.;
RT "Sequences of the genes encoding argininosuccinate synthetase in
RT Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic
RT archaebacteria and mammals.";
RL Gene 95:99-104(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP CHARACTERIZATION, AND CRYSTALLIZATION.
RX PubMed=10666579; DOI=10.1107/s0907444999011816;
RA Lemke C., Yeung M., Howell P.L.;
RT "Expression, purification, crystallization and preliminary X-ray analysis
RT of Escherichia coli argininosuccinate synthetase.";
RL Acta Crystallogr. D 55:2028-2030(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) UNCOMPLEXED AND IN COMPLEX WITH
RP ASPARTATE AND CITRULLINE.
RX PubMed=11738042; DOI=10.1016/s0969-2126(01)00683-9;
RA Lemke C.T., Howell P.L.;
RT "The 1.6 A crystal structure of E. coli argininosuccinate synthetase
RT suggests a conformational change during catalysis.";
RL Structure 9:1153-1164(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP AND CITRULLINE.
RX PubMed=11809762; DOI=10.1074/jbc.m112436200;
RA Lemke C.T., Howell P.L.;
RT "Substrate induced conformational changes in argininosuccinate
RT synthetase.";
RL J. Biol. Chem. 277:13074-13081(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:0000269|PubMed:11738042,
CC ECO:0000269|PubMed:11809762}.
CC -!- INTERACTION:
CC P0A6E4; P0A6E4: argG; NbExp=2; IntAct=EBI-1120296, EBI-1120296;
CC P0A6E4; P24228: dacB; NbExp=2; IntAct=EBI-1120296, EBI-1131834;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The monomer is composed of two major structural domains: a
CC nucleotide-binding domain and a catalytic/multimerization domain.
CC Binding of ATP results in a large rigid body conformational change of
CC the nucleotide binding domain.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; M35236; AAA23482.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57974.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76205.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77217.1; -; Genomic_DNA.
DR PIR; G65107; AJECRS.
DR RefSeq; NP_417640.1; NC_000913.3.
DR RefSeq; WP_000207680.1; NZ_SSZK01000007.1.
DR PDB; 1K92; X-ray; 1.60 A; A=2-447.
DR PDB; 1K97; X-ray; 2.00 A; A=2-447.
DR PDB; 1KP2; X-ray; 2.00 A; A=2-447.
DR PDB; 1KP3; X-ray; 2.00 A; A=2-447.
DR PDBsum; 1K92; -.
DR PDBsum; 1K97; -.
DR PDBsum; 1KP2; -.
DR PDBsum; 1KP3; -.
DR AlphaFoldDB; P0A6E4; -.
DR SMR; P0A6E4; -.
DR BioGRID; 4263121; 37.
DR BioGRID; 851906; 1.
DR DIP; DIP-35842N; -.
DR IntAct; P0A6E4; 14.
DR STRING; 511145.b3172; -.
DR SWISS-2DPAGE; P0A6E4; -.
DR jPOST; P0A6E4; -.
DR PaxDb; P0A6E4; -.
DR PRIDE; P0A6E4; -.
DR EnsemblBacteria; AAC76205; AAC76205; b3172.
DR EnsemblBacteria; BAE77217; BAE77217; BAE77217.
DR GeneID; 947590; -.
DR KEGG; ecj:JW3140; -.
DR KEGG; eco:b3172; -.
DR PATRIC; fig|1411691.4.peg.3559; -.
DR EchoBASE; EB0066; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_1_6; -.
DR InParanoid; P0A6E4; -.
DR OMA; QCEVVTF; -.
DR PhylomeDB; P0A6E4; -.
DR BioCyc; EcoCyc:ARGSUCCINSYN-MON; -.
DR UniPathway; UPA00068; UER00113.
DR EvolutionaryTrace; P0A6E4; -.
DR PRO; PR:P0A6E4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 CDD; cd01999; Argininosuccinate_Synthase; 1.
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; IPR023434; Arginosuc_synth_type_1_subfam.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2123815,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..447
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148695"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 99
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 131
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:11738042"
FT BINDING 135
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:11738042"
FT BINDING 135
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 136
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:11738042"
FT BINDING 139
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 192
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11809762"
FT BINDING 201
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 203
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT BINDING 280
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000269|PubMed:11738042,
FT ECO:0000269|PubMed:11809762"
FT CONFLICT 220
FT /note="I -> N (in Ref. 1; AAA23482)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="G -> D (in Ref. 1; AAA23482)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1KP2"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:1K92"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 295..311
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:1K92"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:1K92"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1K92"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1K92"
SQ SEQUENCE 447 AA; 49898 MW; D5E7E51BD06E1813 CRC64;
MTTILKHLPV GQRIGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE EDYDAIPRRA
MEYGAENARL IDCRKQLVAE GIAAIQCGAF HNTTGGLTYF NTTPLGRAVT GTMLVAAMKE
DGVNIWGDGS TYKGNDIERF YRYGLLTNAE LQIYKPWLDT DFIDELGGRH EMSEFMIACG
FDYKMSVEKA YSTDSNMLGA THEAKDLEYL NSSVKIVNPI MGVKFWDESV KIPAEEVTVR
FEQGHPVALN GKTFSDDVEM MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL
HIAYERLLTG IHNEDTIEQY HAHGRQLGRL LYQGRWFDSQ ALMLRDSLQR WVASQITGEV
TLELRRGNDY SILNTVSENL TYKPERLTME KGDSVFSPDD RIGQLTMRNL DITDTREKLF
GYAKTGLLSS SAASGVPQVE NLENKGQ
