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Database: UniProt
Entry: A6H137_FLAPJ
LinkDB: A6H137_FLAPJ
Original site: A6H137_FLAPJ 
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
//
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