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Database: UniProt
Entry: A0A081CBV8_PSEA2
LinkDB: A0A081CBV8_PSEA2
Original site: A0A081CBV8_PSEA2 
ID   A0A081CBV8_PSEA2        Unreviewed;       361 AA.
AC   A0A081CBV8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:GAK64154.1, ECO:0000313|EMBL:SPO44626.1};
GN   ORFNames=PAN0_004d2363 {ECO:0000313|EMBL:GAK64154.1}, PSANT_02311
GN   {ECO:0000313|EMBL:SPO44626.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64154.1, ECO:0000313|Proteomes:UP000053758};
RN   [1] {ECO:0000313|Proteomes:UP000053758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA   Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA   Morita T.;
RT   "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT   JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT   Lipids.";
RL   Genome Announc. 2:e00878-e00814(2014).
RN   [2] {ECO:0000313|EMBL:GAK64154.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64154.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SPO44626.1, ECO:0000313|Proteomes:UP000325008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC   {ECO:0000313|EMBL:SPO44626.1};
RA   Guldener U.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DF830071; GAK64154.1; -; Genomic_DNA.
DR   EMBL; OOIQ01000004; SPO44626.1; -; Genomic_DNA.
DR   RefSeq; XP_014657794.1; XM_014802308.1.
DR   AlphaFoldDB; A0A081CBV8; -.
DR   GeneID; 26303252; -.
DR   HOGENOM; CLU_042555_4_0_1; -.
DR   OrthoDB; 211603at2759; -.
DR   Proteomes; UP000053758; Unassembled WGS sequence.
DR   Proteomes; UP000325008; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01908; YafJ; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR026869; EgtC-like.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR   PANTHER; PTHR43187:SF1; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR   Pfam; PF13230; GATase_4; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000313|EMBL:GAK64154.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW   Transferase {ECO:0000313|EMBL:GAK64154.1}.
FT   DOMAIN          2..286
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   361 AA;  39922 MW;  241B1DE75942E77D CRC64;
     MCRLLVFKGA DPIQLCHLVT RPAHSIINQA FDSRLRLDAT RAVNGDGFGV GWYDSTRDAE
     LGDAPCIFTS VTPAWNNQNL QRIADKIKSP LVFAHVRAST AGALSETNCH PWRYGRLMWM
     HNGQISDFSR IKRRVLAALP EPLFLFPQGH TDSEFAFAVF LSHLGDPLQT EPFSYKELRD
     AMLATIRDFN GWASEAGIRE PSLMNFCVTD GESIICTRYV SSKSDQAASL YFSSGTSFYE
     HSPGAYRMVK TDKREKIIVV ASEPLTFEKA DWMEIPTNTL VCITPKMNVL QLPILDEFHL
     DRTDQIVRSP TFAMRTGFPP SMSGATAASA EEVKSIAALD GASRGAGAGR NAPIHPVYPC
     P
//
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