ID F7ZZ34_CELGA Unreviewed; 412 AA.
AC F7ZZ34;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=Celgi_1948 {ECO:0000313|EMBL:AEI12450.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12450.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002665; AEI12450.1; -; Genomic_DNA.
DR RefSeq; WP_013883968.1; NC_015671.1.
DR AlphaFoldDB; F7ZZ34; -.
DR STRING; 593907.Celgi_1948; -.
DR KEGG; cga:Celgi_1948; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_11; -.
DR OrthoDB; 9801641at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000000485; 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:UP000000485}.
FT DOMAIN 4..165
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 174..390
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 87
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 119
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
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 127
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 175
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 412 AA; 44780 MW; 799764F9EA2D4138 CRC64;
MTERVVLAYS GGLDTSVGIG WIAEATGAEV IAVAVDVGQG GEDLEVIRRR ALDCGAVEAY
VADARDEFAQ EYCMPALAAN GLYLDRYPLV SALSRPVIVK HLVRAARQFG ATTVAHGCTG
KGNDQVRFEV GITSIAPDLT CLAPVRDLAL TRDKAIEFAE KHQLPIATTK HNPFSIDQNV
WGRAVETGFL EDIWNGPTKD VYTYTDDPTF PPVADEVVIS FEQGVPVALD GVPVTPLQAI
QEMNRRAGAQ GVGRIDIVED RLVGIKSREV YEAPGAIALI TAHQELENVT VEREQARFKR
GVEQRWTELV YDGQWFSPLK RSLDTFIADT QRYVSGDVRL VLHGGRATVT GRRSDTSLYD
FNLATYDTGD TFDQAAARGF IEIYGLSSKL AAARDVRFGN GVDLGSQGGI DA
//
