GTAA_ASPOR
ID GTAA_ASPOR Reviewed; 690 AA.
AC Q2U4L7; Q9UVX9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Glutaminase A {ECO:0000303|PubMed:10952006};
DE EC=3.5.1.2 {ECO:0000269|PubMed:10952006};
DE Flags: Precursor;
GN Name=gtaA {ECO:0000303|PubMed:10952006}; ORFNames=AO090020000289;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-37; 292-298;
RP 407-414; 420-429; 468-496 AND 516-525, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=10952006; DOI=10.1007/s002530000329;
RA Koibuchi K., Nagasaki H., Yuasa A., Kataoka J., Kitamoto K.;
RT "Molecular cloning and characterization of a gene encoding glutaminase from
RT Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 54:59-68(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Glutaminase catalyzes the hydrolysis of glutamine to glutamic
CC acid and plays a key role in nitrogen metabolism. Catalyzes the
CC hydrolysis not only of L-glutamine but also of D-glutamine.
CC {ECO:0000269|PubMed:10952006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000269|PubMed:10952006};
CC -!- ACTIVITY REGULATION: Activity is inhibited by about 80% in the presence
CC of 18% sodium chloride. {ECO:0000269|PubMed:10952006}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for L-glutamine {ECO:0000269|PubMed:10952006};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:10952006};
CC Temperature dependence:
CC Optimum temperature is 37-45 degrees Celsius.
CC {ECO:0000269|PubMed:10952006};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D4AMT2}.
CC -!- BIOTECHNOLOGY: In the fermentation of soy sauce, the traditional
CC Japanese seasoning, glutaminase is one of the most important enzymes in
CC flavor enhancement as it converts glutamine to glutamic acid.
CC {ECO:0000303|PubMed:10952006}.
CC -!- SIMILARITY: Belongs to the fungal glutaminase gtaA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE63498.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP007167; BAE63498.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB029552; BAA86934.1; -; Genomic_DNA.
DR RefSeq; XP_001824631.2; XM_001824579.2.
DR AlphaFoldDB; Q2U4L7; -.
DR SMR; Q2U4L7; -.
DR EnsemblFungi; BAE63498; BAE63498; AO090020000289.
DR GeneID; 5996717; -.
DR KEGG; aor:AO090020000289; -.
DR HOGENOM; CLU_008020_1_1_1; -.
DR SABIO-RK; Q2U4L7; -.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR014870; DUF1793.
DR InterPro; IPR032514; DUF4965.
DR InterPro; IPR033433; DUF5127.
DR Pfam; PF08760; DUF1793; 1.
DR Pfam; PF16335; DUF4965; 1.
DR Pfam; PF17168; DUF5127; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:10952006"
FT CHAIN 21..690
FT /note="Glutaminase A"
FT /id="PRO_5004216798"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 690 AA; 76165 MW; E3D0B17841EEA00D CRC64;
MMHFLSFCLS VASLVSYAGA ASTFSPARPP ALPLAVKSPY LSTWLSAGTD GGNGGYLAGQ
WPTFWFGQVT GWAGQIRVDN STYTWMGAIP NTPTVNQTSF EYTSTSSVFT MRVGDMVEMK
VKFLSPITPD DLRRQSLVFS YLDVDVESID GKAHDIQVYA DISAEWASGD RNAIAQWDYG
VTDDGVAYHK VYRQTQLLFS ENTEQAEWGE WYWATDDQDG LSYQSGPDVD VRGAFAKNGK
LANSDDKNYR AISTNWPVFA FSRDLGSVKT SAGTLFSIGL AQDSAIQYSG KPEGTTVMPS
LWKSYFSTAT AALEFFHHDY AAAAALSKDL DDRISKDSID AAGQDYLTIT SLTVRQVFAA
VQLTGTPEDP YIFMKEISSN GNMNTVDVIF PAHPIFLYTN PELLKLILKP IYEIQENGKY
PNTYAMHDIG THYPNATGHP KGDDEKMPLE ECGNMVIMAL AYAQKAKDND YLSQHYPILN
KWTTYLVEDS IYPANQISTD DFAGSLANQT NLALKGIIGI QAMAVISNTT GHPDDASNHS
SIAKDYIARW QTLGVAHDAN PPHTTLSYGA NETHGLLYNL YADRELGLNL VPQSVYDMQN
TFYPTVKEKY GVPLDTRHVY TKADWELFTA AVASESVRDM FHQALATWIN ETPTNRAFTD
LYDTQTGNYP AGITFIARPV MGGAFALLIL
