ID B8NU21_ASPFN Unreviewed; 863 AA.
AC B8NU21;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=AFLA_101920 {ECO:0000313|EMBL:EED46528.1}, G4B84_009386
GN {ECO:0000313|EMBL:QMW33920.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46528.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED46528.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED46528.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW33920.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW33920.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; EQ963484; EED46528.1; -; Genomic_DNA.
DR EMBL; CP059871; QMW33920.1; -; Genomic_DNA.
DR RefSeq; XP_002384064.1; XM_002384023.1.
DR AlphaFoldDB; B8NU21; -.
DR STRING; 332952.B8NU21; -.
DR EnsemblFungi; EED46528; EED46528; AFLA_101920.
DR VEuPathDB; FungiDB:AFLA_010442; -.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_017290_6_3_1; -.
DR OMA; LEGCPRT; -.
DR OrthoDB; 10308at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 6.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR008147; Gln_synt_N.
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; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
FT DOMAIN 441..533
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 540..863
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 863 AA; 96455 MW; 49E96B97610DEE4E CRC64;
MDLTSLQSLI QTHPLIDNHA HNLLKRDEAC NYAKYPFEQI TSEAQGSALG NATSTLPLHR
AATQLAALYR CASSDWDHVK AARDAWVQRD YDGLIRECLQ GTHTLLLDDL LTDQDIESYE
WHDRFTTSQT KRIVRIEILA AETISTLMRD DARPQEGDVS VLRERWEQFR EGFKQRIAEA
IADPAVVGFK SVICYRTGLN VQPIEDSDDT LLLESFGRTV GQGQGSAYRV EDKRLNDWVV
RQTLNLLQSA KAATASAPNK PLQLHTGLGD NDIDLVLANP AHLQSLIAQY PEVDFVLLHS
SYPYTREAGY LACVYPNVYL DLGEVFPMVS RDAQESILRD SLDIVPTTRL LWSTDGHFFP
ETFYLANKQF RDVMEKVFVD YVHHGDFTVD QAKQAAADIL FHNSNRAYSL NEKLAYEAPV
SANSVSASST ATLDAFMRGN PDVKYIWMQF IDYTNTTRVR MFPVAEFAKI ARKQRRVGIC
LCTQLMLQDD SIAPEGSVTG QFYMEPDLSS LRRNVGIDSK SATVMTYWKT EEGAPLPGCP
RTTLQRVTNN LREHGIEVTC GFEIEVILLK PITNDAGETD YVPVVRNHSW SQMTSDTRKM
VPLLEEIVEA LASIGIHLEQ FHAESAPGQF EFILPPGSPI ATVDTLIKAR QVVTCVAEQH
GLRATLHPRP LPHAAGSASH AHVSIAPPTQ EDAFLAGVMR HYPALAAFTL SQDVSYDRVK
SGLWAGSEWV TWGTQNRETP IRKISPGHWE IKTLDGLANM YFAIAAFLSA GYLGVKENLP
LTVKDCIHDA AKLPQAEREA LGITTELPKS LTQSLDALEA DSALQSIIGE TVVNNYTSVK
RIESKRLLAM DETTRRTWLL ERY
//
