ID Q319R2_PROM9 Unreviewed; 622 AA.
AC Q319R2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
GN OrderedLocusNames=PMT9312_1324 {ECO:0000313|EMBL:ABB50383.1};
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74546 {ECO:0000313|EMBL:ABB50383.1, ECO:0000313|Proteomes:UP000002715};
RN [1] {ECO:0000313|Proteomes:UP000002715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312 {ECO:0000313|Proteomes:UP000002715};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) 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}.
CC -!- SIMILARITY: Belongs to the asparagine synthetase family.
CC {ECO:0000256|ARBA:ARBA00005752}.
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DR EMBL; CP000111; ABB50383.1; -; Genomic_DNA.
DR RefSeq; WP_011376869.1; NC_007577.1.
DR AlphaFoldDB; Q319R2; -.
DR STRING; 74546.PMT9312_1324; -.
DR KEGG; pmi:PMT9312_1324; -.
DR eggNOG; COG0367; Bacteria.
DR HOGENOM; CLU_014658_3_1_3; -.
DR OrthoDB; 9763290at2; -.
DR Proteomes; UP000002715; Chromosome.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR PANTHER; PTHR43284:SF1; ASPARAGINE SYNTHETASE; 1.
DR PANTHER; PTHR43284; ASPARAGINE SYNTHETASE (GLUTAMINE-HYDROLYZING); 1.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW Asparagine biosynthesis {ECO:0000256|PIRSR:PIRSR001589-1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001589-
KW 2};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PIRSR:PIRSR001589-1}; Ligase {ECO:0000313|EMBL:ABB50383.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001589-2}.
FT DOMAIN 2..216
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-1"
FT BINDING 102
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 365..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT SITE 367
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ SEQUENCE 622 AA; 72765 MW; E56B0C1DA66A7879 CRC64;
MCGITGIISF QSSIDPQNIH NMNETLMHRG PDHRDIWINE YSTVFLGHTR LSILDLSDNG
NQPFHSKDGR FHLTFNGEIY NYKNLKDYLK TNGISNFKSN SDTEVLIELI ALRGITNASK
MLNGMFAFAV WDSLEKKIHL VRDRFGEKPL FYTLQKDTLY FGSEIKSILK IPTISKIINK
EALSHYLRFN YIKNPLTIYK DIYKLEPGHI LSIDQNITYK KYSYKNKNKK TIKLANQKEA
EDLLQNQIIK SCLSRTISDV PIACFLSGGI DSSLVTSIIQ RNSKQRIKTF TIGFDDQSID
ESNYAEKIAN FLGTDHTTIN IEEKELLNNI DLQSEIYGEP FADQSSIATN ILCKYASRDV
KVCLSGDGGD EMFIGYDRYY KVNQLRLFLK AIKFYKKFKT IDRILEVLIH KIESNKNFSI
KIDKIIKLIS LLSDANDDNI YEKFNSLYRD QYFPLTPQNN QKHYIYKDLK NIQEMCEYDF
ETYLPDCILT KVDRASMHNS LEVRAPFLDH EIPEIIDSIN PTYKKKLLNR KFILKKLLNK
YLPKNIYERP KKGFSAPLNN WIKGPLKELT LDYLSIESLK KHNLLDIDII ERIKYEHYSG
IRSWHNQIWN LLIFQQWYNK NF
//
