ID A0A1I2CV74_9ACTN Unreviewed; 625 AA.
AC A0A1I2CV74;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
GN ORFNames=SAMN05421541_103225 {ECO:0000313|EMBL:SFE72206.1};
OS Actinoplanes philippinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=35752 {ECO:0000313|EMBL:SFE72206.1, ECO:0000313|Proteomes:UP000199645};
RN [1] {ECO:0000313|EMBL:SFE72206.1, ECO:0000313|Proteomes:UP000199645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43019 {ECO:0000313|EMBL:SFE72206.1,
RC ECO:0000313|Proteomes:UP000199645};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONV01000003; SFE72206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2CV74; -.
DR STRING; 35752.SAMN05421541_103225; -.
DR OrthoDB; 9763290at2; -.
DR Proteomes; UP000199645; Unassembled WGS sequence.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
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; 2.
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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001589-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199645}.
FT DOMAIN 2..197
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 104
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 344..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT SITE 346
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ SEQUENCE 625 AA; 69410 MW; E9587B578B6263BC CRC64;
MCGLSAFVSS RPDPGPLDAT FREAFAAALA TLHHRGPDDT QIEFGDGFAF GFKRLAIIDR
EHSVQPLHYA DRWTVVFNGE IYNYRELRTE LIQQHNAVFA TEGDSEVLAA AFHYWGTLHA
ARDAFGIKPL YMLETADGLY LGSERKALDP FAAPAGAALE TESLAHYLTF QFVPDPMSLH
RHIRRLPPGH RIIWTPGGGI RMHRWFRPSL RPLRVEPEDA FSKIREALTD SVRAHMHAHV
PVGTFLSSGV DSSAIAALAV REKPDIHAFT AGFSAQGYSE IEIAQDTANQ LGIRLTPTVV
SDEDVLTHLP RIIQLLDDPI ADPSLIPLFF LARTASQFVT VVLSGEGSDE LFGGYTIYRE
PLSLGRVDRL PPGMKRGLKH LAEVLPEGVR GRSFLERGTT PIEQRYYGNA RIFDPEEKAR
VMRFTSQPHT AITAPLYAET ADVDDVASMQ YVDLHTWLPG DILVKADRMS MAHSLELRVP
FLDQRVYAAA AGLPTDLKLP PGVTTTKYAL REAMKGIVPE SVREAKKLGF PTPTRLWLRG
QIGDWVDHLL STSQAGDLID LEYVRGLLAE HRAGGPDRSR KVWTVAMFCL WHAIAVEKSI
VVDNPLLPAR VPAPRQEPGL SHIYN
//
