ID A0A147ENF3_9MICO Unreviewed; 473 AA.
AC A0A147ENF3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00014810, ECO:0000256|HAMAP-Rule:MF_00581};
DE EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00581};
DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916, ECO:0000256|HAMAP-Rule:MF_00581};
GN Name=argG {ECO:0000256|HAMAP-Rule:MF_00581};
GN ORFNames=NS354_06960 {ECO:0000313|EMBL:KTR85974.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR85974.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR85974.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR85974.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001891, ECO:0000256|HAMAP-
CC Rule:MF_00581};
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_00581}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00581}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009088, ECO:0000256|HAMAP-
CC Rule:MF_00581}.
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:KTR85974.1}.
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DR EMBL; LDRK01000033; KTR85974.1; -; Genomic_DNA.
DR RefSeq; WP_058593846.1; NZ_LDRK01000033.1.
DR AlphaFoldDB; A0A147ENF3; -.
DR PATRIC; fig|1079994.3.peg.1510; -.
DR OrthoDB; 9801641at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000070810; 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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.400; -; 1.
DR Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00581; Arg_succ_synth_type2; 1.
DR InterPro; IPR023437; Arg_succ_synth_type2_subfam.
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; IPR024074; AS_cat/multimer_dom_body.
DR InterPro; IPR024073; AS_multimer_C_tail.
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_00581};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00581};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00581};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00581};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00581};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00581}; Reference proteome {ECO:0000313|Proteomes:UP000070810}.
FT DOMAIN 14..162
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 191..392
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 99
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 131
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 135
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 135
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 136
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 139
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 192
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 201
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 203
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
FT BINDING 280
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00581"
SQ SEQUENCE 473 AA; 51702 MW; FCBD18D9E3E866E2 CRC64;
MSKVLSSLPV GERVGIAFSG GLDTSCAVAW MREKGAVPCT YTADIGQYDE PDIDGVADRA
KEYGAEIARH VDAKRPLVEE GFVALQTGAF NVRSGGKTYF NTTPLGRAVT GTLLVRAMKE
DGVDIWGDGS TYKGNDIERF YRYGLMANPA LRIYKPWLDH QFVEELGGRH EMSEWLVAHG
YPYRDATEKA YSTDANIWGA THEAKKLEFL DAGLDIVEPI MGVAAWRDDV EVATEEVSVR
FEAGRPVAIN GVEYDDPVAL VLEANAIGGR HGLGVSDQIE NRIIEAKSRG IYEAPGMALL
HITYERLVNA IHNENTLASY HTDGRKLGRL MYEGRWLDPE SLMLRESLQR WVGSAITGEV
TLRLRRGDDY TILNTEGDNL SYHPEKLSME RTVGAAFGPV DRIGQLTMRN LDIADSRQRL
EQYAQLGIVG GSIAELVGQL EQGGAAEIAN AVGGIDEDAD VLGLSAAFDA GTD
//
