ASSY_THEMA
ID ASSY_THEMA Reviewed; 409 AA.
AC Q9X2A1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=TM_1780;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of argininosuccinate synthase (TM1780) from Thermotoga
RT maritima at 1.65 A resolution.";
RL Submitted (MAR-2006) to the PDB data bank.
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|Ref.2}.
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; AE000512; AAD36844.1; -; Genomic_DNA.
DR PIR; H72210; H72210.
DR RefSeq; NP_229577.1; NC_000853.1.
DR RefSeq; WP_004082326.1; NZ_CP011107.1.
DR PDB; 1VL2; X-ray; 1.65 A; A/B/C/D=1-409.
DR PDBsum; 1VL2; -.
DR AlphaFoldDB; Q9X2A1; -.
DR SMR; Q9X2A1; -.
DR STRING; 243274.THEMA_05300; -.
DR EnsemblBacteria; AAD36844; AAD36844; TM_1780.
DR KEGG; tma:TM1780; -.
DR eggNOG; COG0137; Bacteria.
DR InParanoid; Q9X2A1; -.
DR OMA; QCEVVTF; -.
DR OrthoDB; 357142at2; -.
DR UniPathway; UPA00068; UER00113.
DR EvolutionaryTrace; Q9X2A1; -.
DR Proteomes; UP000008183; 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: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; 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..409
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148656"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 85
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 117
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 121
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 121
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 122
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 125
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 178
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 187
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 268
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 280
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1VL2"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1VL2"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 88..107
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1VL2"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:1VL2"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 283..299
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:1VL2"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1VL2"
FT HELIX 383..404
FT /evidence="ECO:0007829|PDB:1VL2"
SQ SEQUENCE 409 AA; 46054 MW; ECCDC8575E962482 CRC64;
MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL KTGASKVYVE
DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ VEIAEKEGAQ YVAHGATGKG
NDQVRFELTY AALNPNLKVI SPWKDPEFLA KFKGRTDLIN YAMEKGIPIK VSKKRPYSED
ENLMHISHEA GKLEDPAHIP DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT
EKTDPLELFE YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM
DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS IYKGNVMPVA
RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH QLVKKGYQR
