ID E8N4B4_ANATU Unreviewed; 424 AA.
AC E8N4B4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:BAJ63278.1};
GN OrderedLocusNames=ANT_12440 {ECO:0000313|EMBL:BAJ63278.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63278.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63278.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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}.
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DR EMBL; AP012029; BAJ63278.1; -; Genomic_DNA.
DR RefSeq; WP_013559666.1; NC_014960.1.
DR AlphaFoldDB; E8N4B4; -.
DR STRING; 926569.ANT_12440; -.
DR GeneID; 78349674; -.
DR KEGG; atm:ANT_12440; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_0; -.
DR InParanoid; E8N4B4; -.
DR OrthoDB; 9801641at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000008922; 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:UP000008922}.
FT DOMAIN 12..173
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 182..399
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 94
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 99
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 130
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 130
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 131
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 134
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 192
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 268
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 280
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ SEQUENCE 424 AA; 47259 MW; 85AD57197CE5CAB9 CRC64;
MPKQTPSTPI KKVVLAYSGG LDTSIIVPWL KENYGCEVIC FTADIGQGEE LSGLPEKAKA
TGASKLYIED LTEEFASQYL FKLLKSGAIY ERHYLLGTSI ARPLIAKHMV EIAHLENADA
VAHGCTGKGN DQVRFELTVM ALDPRLKVIA PWREWNIRSR EDALEYAAAH QVPVSSTLKS
IYSRDRNLWH LSHEGGLLED PWAEPEESMY QITVAPEDAP DTPEYVEITF EEGTPVKLNG
KALSSATLIK ALNEIGGKHG IGRVDMVENR LVGMKSRGVY ETPGGTILMR AHKELEQITL
DRDTLHYKDV MAQRYAELVY YGQWFTPLRE ALDAFFEVTQ KHVTGTVRLK LYKGNIITAG
KKSVFSLYRE DFATFGKDNV YDQSDAAGFI TLFGLPLKVA AMRDIATAVQ IASNAPDYSS
FKRD
//
