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Database: UniProt
Entry: A0A0F7H8G6_SERFO
LinkDB: A0A0F7H8G6_SERFO
Original site: A0A0F7H8G6_SERFO 
ID   A0A0F7H8G6_SERFO        Unreviewed;       405 AA.
AC   A0A0F7H8G6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005};
DE            EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916, ECO:0000256|HAMAP-Rule:MF_00005};
GN   Name=argG {ECO:0000256|HAMAP-Rule:MF_00005,
GN   ECO:0000313|EMBL:VTR37250.1};
GN   ORFNames=NCTC12965_04043 {ECO:0000313|EMBL:VTR37250.1}, WN53_06935
GN   {ECO:0000313|EMBL:AKG68884.1};
OS   Serratia fonticola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG68884.1, ECO:0000313|Proteomes:UP000034699};
RN   [1] {ECO:0000313|EMBL:AKG68884.1, ECO:0000313|Proteomes:UP000034699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG68884.1,
RC   ECO:0000313|Proteomes:UP000034699};
RA   Chan K.-G., Ee R.;
RT   "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VTR37250.1, ECO:0000313|Proteomes:UP000358076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12965 {ECO:0000313|EMBL:VTR37250.1,
RC   ECO:0000313|Proteomes:UP000358076};
RG   Pathogen Informatics;
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004967, ECO:0000256|HAMAP-Rule:MF_00005}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00005}.
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DR   EMBL; CP011254; AKG68884.1; -; Genomic_DNA.
DR   EMBL; CABEEZ010000094; VTR37250.1; -; Genomic_DNA.
DR   RefSeq; WP_024482860.1; NZ_SUPV01000036.1.
DR   AlphaFoldDB; A0A0F7H8G6; -.
DR   STRING; 47917.AV650_04015; -.
DR   GeneID; 30319893; -.
DR   KEGG; sfw:WN53_06935; -.
DR   PATRIC; fig|47917.8.peg.1439; -.
DR   OMA; QCEVVTF; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000034699; Chromosome.
DR   Proteomes; UP000358076; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00005};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00005};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00005};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00005}; Reference proteome {ECO:0000313|Proteomes:UP000034699}.
FT   DOMAIN          8..171
FT                   /note="Arginosuccinate synthase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00764"
FT   DOMAIN          180..397
FT                   /note="Arginosuccinate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20979"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         92
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         97
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         124
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         128
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         128
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         129
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         132
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         181
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         190
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         266
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         278
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   405 AA;  44846 MW;  12C5834EC80423BD CRC64;
     MQNKGIKKIV LAYSGGLDTS AIIPWLKENY GGCEVVAFVA DIGQERGDLE GVEQKALQSG
     ASECHVVDLR EEFIRDYVYP VLQTGALYEG SYLLGTSMAR PIIAKAQVEL ALKVGADALC
     HGATGKGNDQ VRFETTYTAL APHLKVVAPW REWNLRSREA LLDYLKERNI PTTASLEKIY
     SRDENAWHIS TEGGVLESPW NAPNKDCWVW TVDPLEAPDK PEQVTVTVEK GCVVAVNGEA
     MSPYKCLETL NVLGAKHGVG RIDIVENRLV GIKSRGCYET PGGTIMVAAL RGVEQLVLDR
     DSFKWREQLG LEMSYVVYDG RWFAPLRRSI QASAQALAEE VNGEVVLQLY KGQVTAIQKK
     SANSLYSEEF ATFGEDEVYD HSHAGGFIRL FSLSSRIRAL NEKKK
//
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