ASSY_CAMJE
ID ASSY_CAMJE Reviewed; 406 AA.
AC Q9PHK7; Q0PAK8;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=Cj0665c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34806.1; -; Genomic_DNA.
DR PIR; C81415; C81415.
DR RefSeq; WP_002852200.1; NC_002163.1.
DR RefSeq; YP_002344089.1; NC_002163.1.
DR PDB; 4NZP; X-ray; 2.31 A; A=1-406.
DR PDBsum; 4NZP; -.
DR AlphaFoldDB; Q9PHK7; -.
DR SMR; Q9PHK7; -.
DR IntAct; Q9PHK7; 42.
DR STRING; 192222.Cj0665c; -.
DR PaxDb; Q9PHK7; -.
DR PRIDE; Q9PHK7; -.
DR EnsemblBacteria; CAL34806; CAL34806; Cj0665c.
DR GeneID; 904988; -.
DR KEGG; cje:Cj0665c; -.
DR PATRIC; fig|192222.6.peg.657; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_7; -.
DR OMA; QCEVVTF; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000000799; 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..406
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148580"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 91
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 96
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 127
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 127
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 128
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 131
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 181
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 190
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 266
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 278
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:4NZP"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4NZP"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 94..113
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4NZP"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 300..319
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:4NZP"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:4NZP"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:4NZP"
FT HELIX 382..401
FT /evidence="ECO:0007829|PDB:4NZP"
SQ SEQUENCE 406 AA; 45578 MW; 8A1E137AF30EC77F CRC64;
MKNEVKKVVL AYSGGLDTSI ILKWLQDEYN CEVVTFTADI GQGEELEPAR KKALSLGIKE
ENIFIKDLRD EFVKDYVFPM FRANAIYEGE YLLGTSIARP LIAKTQAQIA LQTGADAVSH
GATGKGNDQV RFELGYLAFS PDLKIIAPWR EWDLNSREKL LAYAQKHGID ISKKKGKSPY
SMDANLLHIS YEGLVLEDPA HAPEEDMWRW SKSPKDAPNE SEIIELDFQK GDLVAINGEK
LSPAGLLTKL NELGCKHGIG RLDIVENRYV GMKSRGCYET PGGTILLKAH RALESITLDR
EAAHLKDELM PKYASLIYNG YWFSPERMML QALIDESQIH ANGRVKLELY KGNVMVIGRE
SANDSLFNAA YCTFEEDEVY NQKDAAGFIK LNALRFIIAG KNGRKF
