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Database: UniProt
Entry: A0A0Q9YM24_9COXI
LinkDB: A0A0Q9YM24_9COXI
Original site: A0A0Q9YM24_9COXI 
ID   A0A0Q9YM24_9COXI        Unreviewed;       407 AA.
AC   A0A0Q9YM24;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KRG18330.1};
GN   ORFNames=CC99x_01542 {ECO:0000313|EMBL:KRG18330.1};
OS   Candidatus Berkiella cookevillensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Candidatus Berkiella.
OX   NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG18330.1, ECO:0000313|Proteomes:UP000051494};
RN   [1] {ECO:0000313|EMBL:KRG18330.1, ECO:0000313|Proteomes:UP000051494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC99 {ECO:0000313|EMBL:KRG18330.1,
RC   ECO:0000313|Proteomes:UP000051494};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00005}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRG18330.1}.
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DR   EMBL; LKHV01000007; KRG18330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9YM24; -.
DR   STRING; 437022.CC99x_01542; -.
DR   PATRIC; fig|1590042.3.peg.1567; -.
DR   OrthoDB; 9801641at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000051494; 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:UP000051494}.
FT   DOMAIN          7..167
FT                   /note="Arginosuccinate synthase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00764"
FT   DOMAIN          177..395
FT                   /note="Arginosuccinate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20979"
FT   BINDING         11..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         90
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         121
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
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         125
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         126
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         129
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         178
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         187
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         263
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         275
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   407 AA;  45604 MW;  64E1F103FC455892 CRC64;
     MNTEIRKIVL AYSGGLDTSI MIPWLKEHYQ QAEIIAVICD LGQNEDLVAI KTKAIKSGAS
     KAYLINVQHE FVTQYLWRLV KAGALYEDQY SLGTISRPLI AQKLAEISCM EQADAIAHGA
     TGKGNDQVRF EYTLKALVPH LHIIAPWRIW NISSRQDAIL YAQKHQIDIP ITPKAPYSRD
     ANLWYISHEG GILEDPAQPK PDNLLLITNT LKQTPEHSEE INIDFEQGIP VAINGASMDP
     VTLLNLLNQK AGMHGIGVID MIENRLVGMK IRGVYETPGG TVLYKAHQFL ESLCLDKYTL
     HLKQSLKQNY ANIVYEGRWF SQAKEALDAL IDITQQHVTG TVKLQLFKGN IIFCSMTSPY
     SLHHAGLATF EADTVYNQKD AEGFINLFSL SAKVYGQVHA QEVKYEN
//
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