ID A6H137_FLAPJ Unreviewed; 615 AA.
AC A6H137;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
GN Name=asnB {ECO:0000313|EMBL:CAL44061.1};
GN OrderedLocusNames=FP1997 {ECO:0000313|EMBL:CAL44061.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL44061.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL44061.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44061.1; -; Genomic_DNA.
DR RefSeq; WP_011964098.1; NC_009613.3.
DR RefSeq; YP_001296863.1; NC_009613.3.
DR AlphaFoldDB; A6H137; -.
DR STRING; 402612.FP1997; -.
DR EnsemblBacteria; CAL44061; CAL44061; FP1997.
DR GeneID; 66551820; -.
DR KEGG; fps:FP1997; -.
DR PATRIC; fig|402612.5.peg.2022; -.
DR eggNOG; COG0367; Bacteria.
DR HOGENOM; CLU_014658_3_1_10; -.
DR OMA; CEYVNGL; -.
DR OrthoDB; 9763290at2; -.
DR Proteomes; UP000006394; 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; PF13522; GATase_6; 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:CAL44061.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001589-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006394}.
FT DOMAIN 2..212
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 100
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 361..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT SITE 363
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ SEQUENCE 615 AA; 71388 MW; 8A91B6618A2F94E7 CRC64;
MCGINGILHL SSKLVDKNQL VKMRDVLAHR GPDDAGIFIE KNIGLGHRRL AIIDTSSAGH
QPFYSENGRY VIVFNGEIYN YKDFYAELKD KGVALKSDSD TEVLLKLYEL YGLEILPRLN
GMFAFAIWDK EQKKLVLARD RMGVKPLYYS LYQSTLYFAS EQKALFASGI PIQISESGLE
EYFFNRFVAG ENTLYNHVNK ILPGHYMTIY ENGNSKTTKW WNLKEEIQNH ETIANPKKWF
EETFFESVRL RMVSDVPVGV LLSGGLDSGS ILSSLYHQDY KNIQTFNIGF SEEKHNESYL
AKNITEEYNY EYNSMKVEGD LLYDSLLESS YFQDEPLMHL NEPHLLAVSK LANAKVKVLL
SGEGADELMG GYVRYKALRR PTLLKAISYL SNFNFLNNNP RFNKLLRYSK ITNNSDLVLF
NSTSVYPNDI HEFYGEKKEP INEYRYQLLN EAKELYPNSL QRQALYFDQH TYMCSLLDRN
DRCTMGASIE CREPFLDQRL VAGLGTLDDN WLFSGKKGKY ILKNTMQDKL PQDILNFKKI
GLSVPWENQL LSNDKFKEEL RNFAKSEIFS MPFLENLNGK KIVEQIEKGD KKIIPYIMPL
FMLHIWQKKY FQKFI
//