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Database: UniProt
Entry: A9M4B1
LinkDB: A9M4B1
Original site: A9M4B1 
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   26-NOV-2014, entry version 48.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00581};
DE            EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00581};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00581};
GN   Name=argG {ECO:0000255|HAMAP-Rule:MF_00581};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_00581}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00581}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00581}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00581}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}.
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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; RIVEPIM; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   BioCyc; NMEN374833:GJ7Z-2089-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-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   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. {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING      46     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING     102    102       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     132    132       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING     134    134       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     134    134       ATP. {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING     138    138       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     138    138       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     139    139       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     139    139       ATP. {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING     142    142       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     195    195       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     197    197       ATP. {ECO:0000255|HAMAP-Rule:MF_00581}.
FT   BINDING     204    204       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     206    206       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
FT   BINDING     283    283       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00581}.
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
//
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