ID   A0A068NEY8_9ACTO        Unreviewed;       411 AA.
AC   A0A068NEY8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   18-JAN-2017, entry version 18.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00538879};
DE            EC=6.3.4.5 {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00538882};
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;
OC   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.,
RA   Soby K.M., Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG
RT   27420.";
RL   Genome Announc. 2:e00880-14(2014).
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000256|HAMAP-
CC       Rule:MF_00005, ECO:0000256|SAAS:SAAS00538889}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00005, ECO:0000256|SAAS:SAAS00538878}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00538912}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00538909}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00005,
CC       ECO:0000256|SAAS:SAAS00538902}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of 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   EnsemblBacteria; AIE82188; AIE82188; FB03_01650.
DR   KEGG; asg:FB03_01650; -.
DR   KO; K01940; -.
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-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
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   Pfam; PF00764; Arginosuc_synth; 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|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538918};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538923};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035032};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538880};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538929, ECO:0000313|EMBL:AIE82188.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00005,
KW   ECO:0000256|SAAS:SAAS00538913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035032}.
FT   NP_BIND       9     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING      88     88       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     118    118       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00005}.
FT   BINDING     120    120       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     124    124       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     124    124       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     125    125       Aspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     128    128       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     176    176       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     260    260       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                MF_00005}.
FT   BINDING     272    272       Citrulline. {ECO:0000256|HAMAP-Rule:
FT                                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
//