ID ASSY_BACCN Reviewed; 401 AA.
AC A7GTR5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=Bcer98_3306;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
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DR EMBL; CP000764; ABS23523.1; -; Genomic_DNA.
DR RefSeq; WP_012095764.1; NC_009674.1.
DR AlphaFoldDB; A7GTR5; -.
DR SMR; A7GTR5; -.
DR STRING; 315749.Bcer98_3306; -.
DR GeneID; 56418849; -.
DR KEGG; bcy:Bcer98_3306; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_9; -.
DR OrthoDB; 9801641at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000002300; 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; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.20.5.470; Single helix bin; 1.
DR HAMAP; MF_00005; Arg_succ_synth_type1; 1.
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; IPR023434; Arginosuc_synth_type_1_subfam.
DR InterPro; IPR024074; AS_cat/multimer_dom_body.
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..401
FT /note="Argininosuccinate synthase"
FT /id="PRO_1000073811"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 86
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 118
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
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 122
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 126
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 174
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 183
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 259
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 271
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
SQ SEQUENCE 401 AA; 44796 MW; 42E1D25B4D8E8A0B CRC64;
MEKKKVVLAY SGGLDTSVAI KWLQEKNYDV IALCLDLGEG EDLEFVKEKA LSVGAIKSYM
IDVQEEFMNE YALVALQGHT LYEGKYPLVS ALSRPLIAKK LVEIAELEGA SAVAHGCTGK
GNDQVRFEVS IQALNPYLEV IAPVREWKWS REEEIAYAKE NDVPIPINLD SPFSIDQNLW
GRSNECGILE DPWAAPPEDA YEMTVPLENT PDQPEFVEIG FEEGVPTTLN GTTYSLSQLM
KTLNSLAGKH GIGRIDHVEN RLVGIKSREV YECPAAMTLL TAHKELEDLT LVKEVAHFKP
MMEQKLTELI YNGLWFSPLK QALVAFLQET QKTVSGTVRV KLFKGHAIVE GRKSEYSLYD
ENLATYTVND EFNHDAAVGF ISLFGLPTKV YSQVNQKKVE A
//
