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Database: UniProt
Entry: D1PMI4_9FIRM
LinkDB: D1PMI4_9FIRM
Original site: D1PMI4_9FIRM 
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}.
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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
//
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