ASSY_THET8
ID ASSY_THET8 Reviewed; 400 AA.
AC P59846; Q5SLK9;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005};
DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005};
DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005};
GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00005}; OrderedLocusNames=TTHA0284;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE
RP ANALOGS, AND SUBUNIT.
RX PubMed=11844799; DOI=10.1074/jbc.m112430200;
RA Goto M., Nakajima Y., Hirotsu K.;
RT "Crystal structure of argininosuccinate synthetase from Thermus
RT thermophilus HB8. Structural basis for the catalytic action.";
RL J. Biol. Chem. 277:15890-15896(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATES,
RP AND SUBUNIT.
RX PubMed=12684518; DOI=10.1074/jbc.m213198200;
RA Goto M., Omi R., Miyahara I., Sugahara M., Hirotsu K.;
RT "Structures of argininosuccinate synthetase in enzyme-ATP substrates and
RT enzyme-AMP product forms: stereochemistry of the catalytic reaction.";
RL J. Biol. Chem. 278:22964-22971(2003).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00005};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00005}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005,
CC ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
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DR EMBL; AP008226; BAD70107.1; -; Genomic_DNA.
DR RefSeq; WP_011227831.1; NC_006461.1.
DR RefSeq; YP_143550.1; NC_006461.1.
DR PDB; 1J1Z; X-ray; 2.10 A; A/B/C/D=1-400.
DR PDB; 1J20; X-ray; 2.00 A; A/B/C/D=1-400.
DR PDB; 1J21; X-ray; 2.20 A; A/B/C/D=1-400.
DR PDB; 1KH1; X-ray; 2.30 A; A/B/C/D=1-400.
DR PDB; 1KH2; X-ray; 2.30 A; A/B/C/D=1-400.
DR PDB; 1KH3; X-ray; 2.15 A; A/B/C/D=1-400.
DR PDB; 1KOR; X-ray; 1.95 A; A/B/C/D=1-400.
DR PDBsum; 1J1Z; -.
DR PDBsum; 1J20; -.
DR PDBsum; 1J21; -.
DR PDBsum; 1KH1; -.
DR PDBsum; 1KH2; -.
DR PDBsum; 1KH3; -.
DR PDBsum; 1KOR; -.
DR AlphaFoldDB; P59846; -.
DR SMR; P59846; -.
DR STRING; 300852.55771666; -.
DR DrugBank; DB02267; Argininosuccinate.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR PRIDE; P59846; -.
DR EnsemblBacteria; BAD70107; BAD70107; BAD70107.
DR GeneID; 3168176; -.
DR KEGG; ttj:TTHA0284; -.
DR PATRIC; fig|300852.9.peg.284; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_0; -.
DR OMA; QCEVVTF; -.
DR PhylomeDB; P59846; -.
DR BRENDA; 6.3.4.5; 2305.
DR UniPathway; UPA00068; UER00113.
DR EvolutionaryTrace; P59846; -.
DR Proteomes; UP000000532; 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 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; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..400
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148658"
FT BINDING 6..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005,
FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005,
FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518"
FT BINDING 84
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 89
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005,
FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518"
FT BINDING 116
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 120
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 120
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 121
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 124
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 173
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 182
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 258
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT BINDING 270
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:1KOR"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1KOR"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1J21"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 292..311
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:1KOR"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1KOR"
FT HELIX 373..394
FT /evidence="ECO:0007829|PDB:1KOR"
SQ SEQUENCE 400 AA; 44816 MW; A4DAC90A7C5185C6 CRC64;
MKIVLAYSGG LDTSIILKWL KETYRAEVIA FTADIGQGEE VEEAREKALR TGASKAIALD
LKEEFVRDFV FPMMRAGAVY EGYYLLGTSI ARPLIAKHLV RIAEEEGAEA IAHGATGKGN
DQVRFELTAY ALKPDIKVIA PWREWSFQGR KEMIAYAEAH GIPVPVTQEK PYSMDANLLH
ISYEGGVLED PWAEPPKGMF RMTQDPEEAP DAPEYVEVEF FEGDPVAVNG ERLSPAALLQ
RLNEIGGRHG VGRVDIVENR FVGMKSRGVY ETPGGTILYH ARRAVESLTL DREVLHQRDM
LSPKYAELVY YGFWYAPERE ALQAYFDHVA RSVTGVARLK LYKGNVYVVG RKAPKSLYRQ
DLVSFDEAGG YDQKDAEGFI KIQALRLRVR ALVEREGHGA
