(data stored in ACNUC7421 zone)

SWISSPROT: ASSY_HISS2

ID   ASSY_HISS2              Reviewed;         444 AA.
AC   B0UW58;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 70.
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}; OrderedLocusNames=HSM_0253;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC       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 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}.
DR   EMBL; CP000947; ACA31880.1; -; Genomic_DNA.
DR   RefSeq; WP_012341124.1; NC_010519.1.
DR   SMR; B0UW58; -.
DR   EnsemblBacteria; ACA31880; ACA31880; HSM_0253.
DR   GeneID; 31486533; -.
DR   KEGG; hsm:HSM_0253; -.
DR   HOGENOM; HOG000230094; -.
DR   KO; K01940; -.
DR   OMA; QCEVVTF; -.
DR   OrthoDB; 357142at2; -.
DR   BioCyc; HSOM228400:G1GB8-263-MONOMER; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000008543; 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: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; 3.40.50.620; -; 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   SUPFAM; SSF69864; SSF69864; 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; B0UW58.
DR   SWISS-2DPAGE; B0UW58.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_1000082401"
FT   NP_BIND         18..26
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         44
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         100
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         130
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         132
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         132
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         136
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         136
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         137
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         137
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         140
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         193
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         195
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         202
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         204
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
FT   BINDING         281
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00581"
SQ   SEQUENCE   444 AA;  49607 MW;  E1009DA7889C0D5E CRC64;
     MSNTILQHLP IGQKVGIAFS GGLDTSAALL WMRQKGAVPY AYTANLGQPD EEDYNAIPRK
     AMEYGAEKAR LIDCRNQLAH EGIAAIQCGA FHISTGGVTY FNTTPLGRAV TGTMLVSAMK
     EDDVNIWGDG STFKGNDIER FYRYGLLTNP SLRIYKPWLD NQFIDELGGR QEMSEFLIAN
     GFDYKMSAEK AYSTDSNMLG ATHEAKDLEY LNSGIRIVKP IMGVAFWRDD VTVKAEEVTV
     GFEDGVPVTL NGQSFSSAVE LFLEANRIGG RHGLGMSDQI ENRIIEAKSR GIYEAPGMAL
     LHIAYERLVT AIHNEDTIEQ YRINGLRLGR LLYQGRWFDP QALMLRETAQ RWVARAVTGE
     VTLELRRGND YSILNTVSPN MTYHPERLSM EKVENAPFDP SDRIGQLTMR NLDITDTRDK
     LGIYTHTGLL TVGKDSMLPQ LDKK
//

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