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Database: UniProt
Entry: Q46I72
LinkDB: Q46I72
Original site: Q46I72 
ID   ASSY_PROMT              Reviewed;         400 AA.
AC   Q46I72;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   01-OCT-2014, entry version 64.
DE   RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005};
DE            EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005};
GN   Name=argG {ECO:0000255|HAMAP-Rule:MF_00005};
GN   OrderedLocusNames=PMN2A_1317;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC       diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000255|HAMAP-
CC       Rule:MF_00005}.
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_00005}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}.
CC   -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC       1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
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DR   EMBL; CP000095; AAZ58806.1; -; Genomic_DNA.
DR   RefSeq; WP_011295660.1; NC_007335.2.
DR   RefSeq; YP_292509.1; NC_007335.2.
DR   ProteinModelPortal; Q46I72; -.
DR   STRING; 59920.PMN2A_1317; -.
DR   PRIDE; Q46I72; -.
DR   EnsemblBacteria; AAZ58806; AAZ58806; PMN2A_1317.
DR   GeneID; 3606712; -.
DR   KEGG; pmn:PMN2A_1317; -.
DR   PATRIC; 23026546; VBIProMar14922_2193.
DR   eggNOG; COG0137; -.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; APPEEAY; -.
DR   OrthoDB; EOG6K9QCV; -.
DR   PhylomeDB; Q46I72; -.
DR   BioCyc; PMAR59920:GI1O-2217-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.1260.10; -; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
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   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;
KW   Reference proteome.
FT   CHAIN         1    400       Argininosuccinate synthase.
FT                                /FTId=PRO_0000263951.
FT   NP_BIND      10     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      38     38       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING      89     89       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     119    119       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING     121    121       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     125    125       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     125    125       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     126    126       Aspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     129    129       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     177    177       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     186    186       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     262    262       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     274    274       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   400 AA;  44116 MW;  305D70454D2FBCBB CRC64;
     MGKANKVVLA YSGGVDTSVC IPYLKEEYGV EHVIAFAADL GQGDELDEIK KKAISAGASQ
     SLIGNLVKPF IEDFAFPAIR SNALYQGRYP LSTALARPLI AKKLVEIARE LNADGVAHGC
     TGKGNDQVRF DVTIGALAPD LQLLTPAREW GMSREETIAY GEKYGIVPPV SKKNPYSIDL
     NLLGRSIEAG PLEDPFQMPS EEVFGITSSI ADSPNEPEIA DILFENGYPV AINGEEMEPV
     SLIKKANSLA GKHGFGRLDI IEDRVVGIKS REIYETPGLL LLIKAHQEIE SLTLPADLLD
     TKSRLERQWA DLVYKGFWFS PLKEALDGFI NYSQKQVNGT VRVRLFKGNV DVIGRKSKEN
     SLYISDMSTY GSEDKFNHKS AEGFIYVWGL PSRIWSWINK
//
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