(data stored in ACNUC7421 zone)

SWISSPROT: ASSY_AERHH

ID   ASSY_AERHH              Reviewed;         411 AA.
AC   A0KFV3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
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=AHA_0596;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC         arginino)succinate + AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472,
CC         ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; CP000462; ABK39577.1; -; Genomic_DNA.
DR   RefSeq; WP_011704563.1; NC_008570.1.
DR   RefSeq; YP_855129.1; NC_008570.1.
DR   SMR; A0KFV3; -.
DR   STRING; 380703.AHA_0596; -.
DR   EnsemblBacteria; ABK39577; ABK39577; AHA_0596.
DR   GeneID; 4489263; -.
DR   KEGG; aha:AHA_0596; -.
DR   PATRIC; fig|380703.7.peg.593; -.
DR   eggNOG; ENOG4105CDH; Bacteria.
DR   eggNOG; COG0137; LUCA.
DR   HOGENOM; HOG000230093; -.
DR   KO; K01940; -.
DR   OMA; PAREWGM; -.
DR   BioCyc; AHYD380703:G1G7B-597-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000000756; 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; 3.40.50.620; -; 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   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;
DR   PRODOM; A0KFV3.
DR   SWISS-2DPAGE; A0KFV3.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    411       Argininosuccinate synthase.
FT                                /FTId=PRO_0000321297.
FT   NP_BIND      10     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00005}.
FT   BINDING      37     37       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      94     94       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     178    178       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     187    187       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     263    263       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
FT   BINDING     275    275       Citrulline. {ECO:0000255|HAMAP-
FT                                Rule:MF_00005}.
SQ   SEQUENCE   411 AA;  45190 MW;  99C9323F9F0BFE8B CRC64;
     MSGINKIVLA YSGGLDTSAI IPWLKENYDA EIIAFVADVG QERDDLEGIE QKAIASGATK
     CIVKDLREEF VKEYVYPTLK TGAVYEGTYL LGTSMARPVI AKAMVEAALA EGADAISHGC
     TGKGNDQVRF EGAVAALAPQ LKVIAPWRLW DMRSREDLLA YLETRNIPCK ATLKKIYSRD
     ANAWHISTEG GELESTWNEP SEAVWQWTVP AEQAPDQPEY VKLTVAQGEV VAVDDQPLSP
     HQILTTLNER AGKHGVGRID ITENRMVGMK SRGCYETPGG TVMVAALRAV EELVLDRPTR
     AWREKLGAEF SHLVYDGRWF TPLCKAIVAS ANAIAEDLDG EVVLKMYKGQ VTAVQKKSPN
     SLYSEDFATF GADEVYDQSH AEGFIRLYTL ASRIRAMKEQ HQAIGGDHTH G
//

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