ASSY_LEGPH
ID ASSY_LEGPH Reviewed; 405 AA.
AC Q5ZY78;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=lpg0494;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU26591.1; -; Genomic_DNA.
DR RefSeq; WP_010946242.1; NC_002942.5.
DR RefSeq; YP_094538.1; NC_002942.5.
DR PDB; 6XNQ; X-ray; 1.95 A; A/B/C/D=1-405.
DR PDB; 7K5Z; X-ray; 1.85 A; A/B/C/D=1-405.
DR PDBsum; 6XNQ; -.
DR PDBsum; 7K5Z; -.
DR AlphaFoldDB; Q5ZY78; -.
DR SMR; Q5ZY78; -.
DR STRING; 272624.lpg0494; -.
DR PaxDb; Q5ZY78; -.
DR EnsemblBacteria; AAU26591; AAU26591; lpg0494.
DR GeneID; 66489688; -.
DR KEGG; lpn:lpg0494; -.
DR PATRIC; fig|272624.6.peg.515; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_6; -.
DR OMA; QCEVVTF; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000000609; 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..405
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148604"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 90
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 121
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 125
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 125
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 126
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 129
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 178
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 187
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 263
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT BINDING 275
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:7K5Z"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:7K5Z"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6XNQ"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:7K5Z"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:7K5Z"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:7K5Z"
FT HELIX 390..398
FT /evidence="ECO:0007829|PDB:7K5Z"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:7K5Z"
SQ SEQUENCE 405 AA; 44985 MW; 6A76E7D62947DC56 CRC64;
MKKVIKKIAL AYSGGLDTSI MIPWLKEHYE HAEVIAVICD LGQQEDLDAI KNKALKSGAS
KAYVVDVKNE FATQYLWPLV KSGALYEDQY ILGTISRPLI AQKLVEIALT EQVNAVAHGA
TGKGNDQVRF EYSIKALAPQ LEIIAPWRTW DIKSRQEAIV YAKAHGIEVP VTPKAPYSRD
HNIWYISHEG GVLEDPSQEM PNDVLLMTAP VSQTPDEEEV VVLDFKKGVP VALNGQELSP
VDLLNSLNQK AGQHGIGVAD IVENRLVGMK IRGIYEAPAA AVLYKAHKLL ESLCLTRSTL
HLKQSLQQTY ANLVYEGRWF SQTKQALDAF IDVTQQHVTG CVKLKLFKGN IIPAGMHSPY
SLHHPELATF EEDNVYNQKD AEGFINLFSL SAKIYSQVHQ GGNYD
