ID   ASSY_PARP8              Reviewed;         444 AA.
AC   B2JP23;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=Bphy_5499;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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}.
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; CP001044; ACC74576.1; -; Genomic_DNA.
DR   RefSeq; WP_012404740.1; NZ_CADFGH010000008.1.
DR   AlphaFoldDB; B2JP23; -.
DR   SMR; B2JP23; -.
DR   STRING; 391038.Bphy_5499; -.
DR   KEGG; bph:Bphy_5499; -.
DR   eggNOG; COG0137; Bacteria.
DR   HOGENOM; CLU_032784_4_1_4; -.
DR   OrthoDB; 9801641at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000001192; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_1000129742"
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   444 AA;  49211 MW;  59750442769CEE35 CRC64;
     MSTILESLPT GQKVGIAFSG GLDTSAALHW MRLKGAVPYA YTANLGQPDE DDYDSIPRRA
     TEYGAEGARL IDCRAQLVAE GIAALQSGAF HISTAGVTYF NTTPIGRAVT GTMLVAAMKE
     DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ TFIDELGGRA EMSEFMRQSG
     FAYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV QIAKEEVTVR
     FEEGQPVALN GKTFPNAVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL
     FAAYERLVTG IHNEDTIEQY RESGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV
     TLELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD RIGQLTMRNL DITDTRDKLR
     VYSQVGLLAP GEASALPQIK GDKE
//