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Database: UniProt
Entry: D7CJ36_SYNLT
LinkDB: D7CJ36_SYNLT
Original site: D7CJ36_SYNLT 
ID   D7CJ36_SYNLT            Unreviewed;       401 AA.
AC   D7CJ36;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
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   OrderedLocusNames=Slip_2172 {ECO:0000313|EMBL:ADI02914.1};
OS   Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophothermus.
OX   NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI02914.1, ECO:0000313|Proteomes:UP000000378};
RN   [1] {ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   DOI=10.4056/sigs.1233249;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1T).";
RL   Stand. Genomic Sci. 3:267-275(2010).
RN   [2] {ECO:0000313|EMBL:ADI02914.1, ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   PubMed=21304731;
RA   Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1).";
RL   Stand. Genomic Sci. 3:268-275(2010).
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; CP002048; ADI02914.1; -; Genomic_DNA.
DR   RefSeq; WP_013176316.1; NC_014220.1.
DR   AlphaFoldDB; D7CJ36; -.
DR   STRING; 643648.Slip_2172; -.
DR   KEGG; slp:Slip_2172; -.
DR   eggNOG; COG0137; Bacteria.
DR   HOGENOM; CLU_032784_4_2_9; -.
DR   OMA; QCEVVTF; -.
DR   OrthoDB; 9801641at2; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000000378; 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; 3.90.1260.10; 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:UP000000378}.
FT   DOMAIN          3..164
FT                   /note="Arginosuccinate synthase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00764"
FT   DOMAIN          173..390
FT                   /note="Arginosuccinate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20979"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         85
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
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         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         117
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
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         121
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         122
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         174
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         183
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         259
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT   BINDING         271
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   401 AA;  44926 MW;  7FAB66A47F51FF10 CRC64;
     MDKVVLAYSG GLDTSIIIPW LKENYGYEVI AMCADLGQGE ELAGLEEKAL RSGAGKVYIE
     DVREEFVRDY IFPVLRAGAI YEGKYLLGTS FARPLIARKL VEIAEKEGAT AVAHGATGKG
     NDQVRFEVSV KALNPELKII APWREWDIKS REDAIEYAQK HNVPVPVTKK SIYSRDRNLW
     HLSHEGGELE DPMQEPKDEM YLLTVPPEKA PDHPTYVEIE YEQGVPVAID GQMMGPVELI
     EKLNHLAGAN GVGIVSLVEN RLVGMKSRGV YECPGGTVLF TSHRELENLT LDRRTMHFKE
     QVAILYAELV YDGLWFSQLK EALDAFVAKT QETVTGKVRV KLYKGNCTPV GAESPYSLYR
     HDLATFGESD FYNQKDAEGF INLFGLPLKV RALMERKVGK R
//
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