ID D1PMI4_9FIRM Unreviewed; 615 AA.
AC D1PMI4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:EFB75769.1};
GN ORFNames=SUBVAR_05544 {ECO:0000313|EMBL:EFB75769.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75769.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB75769.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75769.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFB75769.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACBY02000023; EFB75769.1; -; Genomic_DNA.
DR RefSeq; WP_007046929.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PMI4; -.
DR STRING; 411471.SUBVAR_05544; -.
DR GeneID; 78305749; -.
DR eggNOG; COG0367; Bacteria.
DR HOGENOM; CLU_014658_3_2_9; -.
DR OrthoDB; 9763290at2; -.
DR Proteomes; UP000003438; Unassembled WGS sequence.
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:EFB75769.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001589-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT DOMAIN 2..217
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 103
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 379..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT SITE 381
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ SEQUENCE 615 AA; 69262 MW; EC3156BB483AFF8D CRC64;
MCGIAGQIGR NPRAIQGNYA AYCAMQRTMA RRGPDQRGMY ISGRAALIHA RLAVVDLENG
CQPMQLDWQG ESYTLVYNGE LYNTPELRAA LENRGHRFIG HSDTEVLLHA YAEWGASCVD
RFNGIFAFAV WEAHGGKLFL ARDRCGVKPL FYAKTRDSLI FGSEIKTVLA HPAVPPRVDA
NGLAEVLLLG PGRIPGSGVF QNVHELLPGQ YGIYEADSGH LLLHRYWQLV DHEHPDDFTA
TAHKVRDLLM DAIQRQLVSD VPVATFLSGG LDSSLISAVA DAQFTAQGKT LHTFSVGYKD
NKRYFHETKF QPGPDAPFIR MMNDFLHAEH HWITLDTPEL VPALYAAVEA RDLPGMADVD
ASLLAFCRYI KPHATVALSG ECADEIFGGY PWYRDPTIRE KYGFPWAQST AYRASFLKPG
VLDGIDPEGF VDAQYQKTLA ETSVRPGLSP LEQRMRQMMS LNFHWFMQTL LDRKDRMSMY
SGLEVRVPFC DYRIAEYLYS VPWEFKDYQG KEKGLLREAM TGVLPPEVLW RKKSPYPKTW
NPGYLAAVSA ELTKVLEDPA APLLRIIRAE ALEKLLASGA DNPVPWYGQL MTTPQTIAWF
LQLNYWLQTY QVELV
//