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ASSY_BRAHW
ID   ASSY_BRAHW              Reviewed;         406 AA.
AC   C0R1H5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=BHWA1_01491;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT   intestine.";
RL   PLoS ONE 4:E4641-E4641(2009).
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_00005};
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_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 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}.
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DR   EMBL; CP001357; ACN83963.1; -; Genomic_DNA.
DR   RefSeq; WP_012671005.1; NC_012225.1.
DR   AlphaFoldDB; C0R1H5; -.
DR   SMR; C0R1H5; -.
DR   STRING; 565034.BHWA1_01491; -.
DR   EnsemblBacteria; ACN83963; ACN83963; BHWA1_01491.
DR   GeneID; 63962587; -.
DR   KEGG; bhy:BHWA1_01491; -.
DR   eggNOG; COG0137; Bacteria.
DR   HOGENOM; CLU_032784_4_2_12; -.
DR   OMA; QCEVVTF; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000001803; 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   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;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding.
FT   CHAIN           1..406
FT                   /note="Argininosuccinate synthase"
FT                   /id="PRO_1000191882"
FT   BINDING         8..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         86
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         91
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         118
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         122
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         122
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         123
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         126
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         175
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         184
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         261
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
FT   BINDING         273
FT                   /ligand="L-citrulline"
FT                   /ligand_id="ChEBI:CHEBI:57743"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00005"
SQ   SEQUENCE   406 AA;  45587 MW;  F85996AB841BFAE9 CRC64;
     MKKKLVLAYS GGLDTTVIIP WLKENYDYDV IAVCVDVGQG TETDGLEEKA LKTGAVKYRL
     VKCEDEFVTD YIYPIVKAEA TYEDKYLLGT SAARPLIAKK LVEVALEEGA TAIAHGATGK
     GNDQVRFELT VKALAPNFEI IAPWREWNIS SREEEIKYLE DRNIEVPMKK DDSYSRDKNL
     WHLSHEGLEL EDPANMPNYE RLLKLSNTIE NAPNEGQFVE LEFEKGIPTK VDGKTFSPSD
     LVKYLNEIGG KHAVGIVDLL ENRVVGIKCR GVYETPGGTI LYAAHREIEH LCLDRETLYF
     KHVVSHKLTD LVYSGRWFTP LREALCAFID STQQTVTGKV KLKLYKGNII PAGVTSPYSL
     YNQSLASFTT GELYDHHDAQ GFITLFGLPL KVNALMKEQA KKMGLK
 
 
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