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Database: UniProt
Entry: Q54991_STRRM
LinkDB: Q54991_STRRM
Original site: Q54991_STRRM 
ID   Q54991_STRRM            Unreviewed;        81 AA.
AC   Q54991;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE            EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
DE   Flags: Fragment;
OS   Streptomyces rimosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1927 {ECO:0000313|EMBL:AAA03335.1};
RN   [1] {ECO:0000313|EMBL:AAA03335.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=15883 {ECO:0000313|EMBL:AAA03335.1};
RA   Hunter I.S.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate +
CC         H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001778};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (L-Gln route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005187}.
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DR   EMBL; U01666; AAA03335.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54991; -.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR43284:SF1; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR43284; ASPARAGINE SYNTHETASE (GLUTAMINE-HYDROLYZING); 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
FT   DOMAIN          2..81
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   NON_TER         81
FT                   /evidence="ECO:0000313|EMBL:AAA03335.1"
SQ   SEQUENCE   81 AA;  8713 MW;  67B372B720EF1B80 CRC64;
     MCGIAGWIDF ERNLAQERAT AWAMTDTMAC RGPDDAGLWT GGHAALGHRR LAVIDPAHGR
     QPMHSTLPDG TSHVITFSGE I
//
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