ID   ASSY_RALPJ              Reviewed;         445 AA.
AC   B2UBA3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00581};
DE            EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00581};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00581};
GN   Name=argG {ECO:0000255|HAMAP-Rule:MF_00581};
GN   OrderedLocusNames=Rpic_2829;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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_00581};
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_00581}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00581}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00581}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}.
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DR   EMBL; CP001068; ACD27952.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UBA3; -.
DR   SMR; B2UBA3; -.
DR   STRING; 402626.Rpic_2829; -.
DR   KEGG; rpi:Rpic_2829; -.
DR   eggNOG; COG0137; Bacteria.
DR   HOGENOM; CLU_032784_4_1_4; -.
DR   UniPathway; UPA00068; UER00113.
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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.400; -; 1.
DR   Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00581; Arg_succ_synth_type2; 1.
DR   InterPro; IPR023437; Arg_succ_synth_type2_subfam.
DR   InterPro; IPR048268; Arginosuc_syn_C.
DR   InterPro; IPR048267; Arginosuc_syn_N.
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   NCBIfam; TIGR00032; argG; 1.
DR   PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1.
DR   PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1.
DR   Pfam; PF20979; Arginosuc_syn_C; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 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.
FT   CHAIN           1..445
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_1000129760"
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         99
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         131
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         135
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         135
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         136
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         139
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         192
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         201
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         203
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         280
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
SQ   SEQUENCE   445 AA;  49292 MW;  63F56DB32F7BDE4A CRC64;
     METILQHVPV GQKVGIAFSG GLDTSAALRW MKNKGALPYA YTANLGQPDE EDYDAIPRKA
     MEYGAEKARL IDCRPQLANE GIAAIQSGAF HISTGGITYF NTTPLGRAVT GTMLVAAMKE
     DDVNIWGDGS TFKGNDIERF YRYGLLTNPA LKIYKPWLDQ AFIDELGGRA EMSAFMTKEG
     FGYKMSAEKA YSTDSNMLGA THEAKDLEHL NSGIRIVNPI MGVAFWKPEV EVKAEEVSIT
     FDEGRPVAVN GREIADPVEM FLELNRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL
     HIAYERLVTG IHNEDTIEQY RINGLRLGRL LYQGRWFDPQ AIMLRETAQR WVARAVTGTV
     TLELRRGNDY SILNTESPNL TYAPERLSME KVEDAPFSPA DRIGQLTMRN LDLMDTRDKL
     AIYSKAGLLS LGTANALPQL DGGKK
//