ASSY_BORPE
ID ASSY_BORPE Reviewed; 445 AA.
AC Q7VTJ9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=BP3537;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640421; CAE43796.1; -; Genomic_DNA.
DR RefSeq; NP_882052.1; NC_002929.2.
DR RefSeq; WP_003820367.1; NZ_CP039022.1.
DR PDB; 5US8; X-ray; 2.15 A; A/B=1-445.
DR PDB; 6E5Y; X-ray; 1.50 A; A=1-445.
DR PDBsum; 5US8; -.
DR PDBsum; 6E5Y; -.
DR AlphaFoldDB; Q7VTJ9; -.
DR SMR; Q7VTJ9; -.
DR STRING; 257313.BP3537; -.
DR GeneID; 45390065; -.
DR KEGG; bpe:BP3537; -.
DR PATRIC; fig|257313.5.peg.3829; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_1_4; -.
DR OMA; QCEVVTF; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000002676; 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: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; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00581; Arg_succ_synth_type2; 1.
DR InterPro; IPR023437; Arg_succ_synth_type2_subfam.
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 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..445
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148692"
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"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5US8"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5US8"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:6E5Y"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 295..311
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:6E5Y"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:6E5Y"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:6E5Y"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6E5Y"
SQ SEQUENCE 445 AA; 49323 MW; 81278F1EBC07CE61 CRC64;
MTTILPNLPT GQKVGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE PDYDEIPRRA
MQYGAEAARL VDCRAQLVAE GIAALQAGAF HISTAGLTYF NTTPIGRAVT GTMLVAAMKE
DGVNIWGDGS TFKGNDIERF YRYGLLTNPD LKIYKPWLDQ TFIDELGGRA EMSEYMRQAG
FDYKMSAEKA YSTDSNMLGA THEAKDLELL SAGIRIVQPI MGVAFWQDSV QIKAEEVTVR
FEEGQPVALN GVEYADPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL
FIAYERLVTG IHNEDTIEQY RENGRKLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV
TLELRRGNDY SLLNTESANL TYAPERLSME KVENAPFTPA DRIGQLTMRN LDIVDTREKL
FTYVKTGLLA PSAGSALPQI KDGKK
