ID A0A401KJ53_ASPAW Unreviewed; 838 AA.
AC A0A401KJ53;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=AAWM_02315 {ECO:0000313|EMBL:GCB19430.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB19430.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB19430.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB19430.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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:GCB19430.1}.
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DR EMBL; BDHI01000002; GCB19430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KJ53; -.
DR STRING; 105351.A0A401KJ53; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR Gene3D; 2.40.37.20; D-serine dehydratase-like domain; 1.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR Pfam; PF14031; D-ser_dehydrat; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01119; D-ser_dehydrat; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT DOMAIN 117..504
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 838 AA; 92122 MW; FA107AB91956ECBB CRC64;
MATTITAEDL PNLLANDIKV KVAGVDCDGI LRGKVMAKEK FLGIAQKGFG FSSAVFGWDM
QDVLYTTEAN IAPADSGYVD FLAVPDLNSF RRIPWEDDIP FFLVRFVQND KPVSADGRSM
LRSICDKLAA NNCKGMAGVE LEFMNFQTPS EDGYGANGSQ TRDIAAFLDK NAPGALRPLT
AGSFSYSATR PVAYKKYFYD IFDTSARFNC GIEGWHTEGG PGVYEAALKV CDVSDMADKV
SLFKLLAKSI GLEHGITPCF MAKPMQGQPG SSGHIHVSLT DLEGKNLFAR DTPDPNSPWS
DAAGLSDLGR HFLAGVLEAL PDIMPLFAPT INSYKRLVEN FWAPVNISWG LEDRMASVRI
ITPPVCKPGA TRFEVRIPGA DLHPHYALSV ILAAGWRGVE KKLDIKVPPV NVQKAEKIKA
ELLPNTLEEA LKRFSDKGSV AREILDPEFV DFFTATREHE LRVWREAVTD WEFKRYIETT
LEITRLMLAN GLHRGLIAST LSELRGVLPL AEEGILNEAL YGLPIYPSAL PHLHSIRQSH
PNLNILIMVD SPQHIPIIEA FNKSTPDVRP WPVFIKLDVG SRRAGVDVYS PDSGPELEEL
VNAVEESSAV ELYGFYCHAG HSYSSKGEEE AGRVLGSEVG GVLRAVKLIN SEGKGEKKRK
IVLSIGSTPT AHVVRQVKQY LTEERNVNSA VDVDVEVHAG NYPTNDLQQL STDLITPADL
AVRVLAEICS VYPRRNEALI NAGTVALSKE TSAVPGFGRL VDKPEWGLVR MSQEHGILGL
LSGESEGEGK KVDDVFHVGQ KVMLHCQHAC ITAAQHFVYY VVDGEEVVRE TWVPWKGW
//
