ID   A0A068NEY8_9ACTO        Unreviewed;       411 AA.
AC   A0A068NEY8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   14-DEC-2022, entry version 35.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000256|HAMAP-Rule:MF_00005};
DE            EC=6.3.4.5 {ECO:0000256|HAMAP-Rule:MF_00005};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00005};
GN   Name=argG {ECO:0000256|HAMAP-Rule:MF_00005};
GN   ORFNames=FB03_01650 {ECO:0000313|EMBL:AIE82188.1};
OS   Actinotignum schaalii.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinotignum.
OX   NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82188.1, ECO:0000313|Proteomes:UP000035032};
RN   [1] {ECO:0000313|EMBL:AIE82188.1, ECO:0000313|Proteomes:UP000035032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82188.1,
RC   ECO:0000313|Proteomes:UP000035032};
RX   PubMed=25189588;
RA   Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA   Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA   Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL   Genome Announc. 2:e00880-14(2014).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00005}.
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DR   EMBL; CP008802; AIE82188.1; -; Genomic_DNA.
DR   RefSeq; WP_026428863.1; NZ_CP008802.1.
DR   AlphaFoldDB; A0A068NEY8; -.
DR   EnsemblBacteria; AIE82188; AIE82188; FB03_01650.
DR   KEGG; asg:FB03_01650; -.
DR   OrthoDB; 357142at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000035032; 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; ARGININOSUCCINATE SYNTHASE; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 1.
DR   TIGRFAMs; TIGR00032; argG; 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}.
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         88
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         120
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
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         124
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         125
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         176
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         260
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         272
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   411 AA;  45046 MW;  2F4BFF9524683C8E CRC64;
     MAKERVVLAY SGGLDTSVAI GWIGERTGAE VITVAVDVGQ GGEDLETIRQ RALDCGAVEA
     YIADARDEFA SEYCMPALKA GALYMDAYPL ISAISRPVIV KHLVAAARQF GATTVAHGCT
     GKGNDQVRFE NGITQLGPDL ACLSPVRDLA LTREFAIDYA NKHNLPIETT HHNPFSIDQN
     VWGRAIETGY LEDLWNAPTK DVYTYTDDPT YPPLPDEVII TFEGGIPVKI DGEAVTPLQA
     IEQLNKRAGK QGIGRIDVVE DRYVGIKSRE IYEAPGAMAL LTAHKELENV TMDREQARFK
     RTVTDRWADI VYEGQWFSPL KRSLDAYIED TQRYVSGDIR MVMHGGRATV TGRRSDASLY
     DFNLATYDAG DSFDQSHAKG FIELTGLPAK LAAARDVTFG RGVAIPPARL N
//