ID ASSY_NEIM0 Reviewed; 447 AA.
AC A9M4B1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
DE RecName: Full=Argininosuccinate synthase;
DE EC=6.3.4.5;
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=argG; OrderedLocusNames=NMCC_2087;
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=374833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442;
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X.,
RA Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y.,
RA Shao Z., Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC diphosphate + N(omega)-(L-arginino)succinate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC 2 subfamily.
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DR EMBL; CP000381; ABX74205.1; -; Genomic_DNA.
DR RefSeq; YP_001600172.1; NC_010120.1.
DR ProteinModelPortal; A9M4B1; -.
DR SMR; A9M4B1; 6-445.
DR STRING; 374833.NMCC_2087; -.
DR PRIDE; A9M4B1; -.
DR EnsemblBacteria; ABX74205; ABX74205; NMCC_2087.
DR GeneID; 5795435; -.
DR KEGG; nmn:NMCC_2087; -.
DR PATRIC; 20349366; VBINeiMen117761_2568.
DR eggNOG; COG0137; -.
DR HOGENOM; HOG000230094; -.
DR KO; K01940; -.
DR OMA; GGRKEMS; -.
DR ProtClustDB; PRK05370; -.
DR BioCyc; NMEN374833:GJ7Z-2089-MONOMER; -.
DR UniPathway; UPA00068; UER00113.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 1.10.287.400; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00581; Arg_succ_synth_type2; 1; -.
DR InterPro; IPR023437; Arg_succ_synth_type2_subfam.
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 PANTHER; PTHR11587; PTHR11587; 1.
DR Pfam; PF00764; Arginosuc_synth; 1.
DR TIGRFAMs; TIGR00032; argG; 1.
DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1 447 Argininosuccinate synthase.
FT /FTId=PRO_1000082403.
FT NP_BIND 20 28 ATP (By similarity).
FT BINDING 46 46 ATP (By similarity).
FT BINDING 102 102 Citrulline (By similarity).
FT BINDING 132 132 ATP; via amide nitrogen (By similarity).
FT BINDING 134 134 Aspartate (By similarity).
FT BINDING 134 134 ATP (By similarity).
FT BINDING 138 138 Aspartate (By similarity).
FT BINDING 138 138 Citrulline (By similarity).
FT BINDING 139 139 Aspartate (By similarity).
FT BINDING 139 139 ATP (By similarity).
FT BINDING 142 142 Citrulline (By similarity).
FT BINDING 195 195 Citrulline (By similarity).
FT BINDING 197 197 ATP (By similarity).
FT BINDING 204 204 Citrulline (By similarity).
FT BINDING 206 206 Citrulline (By similarity).
FT BINDING 283 283 Citrulline (By similarity).
SQ SEQUENCE 447 AA; 49650 MW; 94FECD825352EA06 CRC64;
MSQNHTILQS LPVGQKVGIA FSGGLDTSAA LLWMKLKGAL PYAYTANLGQ PDEDDYNAIP
KKAMEYGAEN ARLIDCRAQL AHEGIAAIQC GAFHVSTGGI AYFNTTPLGR AVTGTMLVSA
MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT NPALKIYKPW LDQQFIDELG GRHEMSEFLI
ANGFNYKMSV EKAYSTDSNM LGATHEAKDL EFLNSGIKIV KPIMGVAFWD ENVEVSPEEV
SVRFEEGVPV ALNGKEYADP VELFLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM
ALFHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET AQRWVAKAIT
GEVTLELRRG NDYSILNTES PNLTYQPERL SMEKVEDAAF TPLDRIGQLT MRNLDITDTR
AKLGIYSQSG LLSLGEGSVL PQLGNKQ
//
