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Database: UniProt
Entry: G3B1T1_CANTC
LinkDB: G3B1T1_CANTC
Original site: G3B1T1_CANTC 
ID   G3B1T1_CANTC            Unreviewed;       348 AA.
AC   G3B1T1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=N-terminal nucleophile aminohydrolase {ECO:0000313|EMBL:EGV64525.1};
GN   ORFNames=CANTEDRAFT_92757 {ECO:0000313|EMBL:EGV64525.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV64525.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR   EMBL; GL996515; EGV64525.1; -; Genomic_DNA.
DR   RefSeq; XP_006685331.1; XM_006685268.1.
DR   AlphaFoldDB; G3B1T1; -.
DR   STRING; 590646.G3B1T1; -.
DR   GeneID; 18250226; -.
DR   KEGG; cten:CANTEDRAFT_92757; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   HOGENOM; CLU_042555_4_0_1; -.
DR   OrthoDB; 211603at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase 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   Hydrolase {ECO:0000313|EMBL:EGV64525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT   DOMAIN          2..250
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   348 AA;  39012 MW;  CAC683B670174806 CRC64;
     MCRFMIFKGK EPMVLEDLLT KPAHSIINQS FDSRLRLDMR NPVNGDGFGV GYYSSSQHPC
     VFKAITPAWN NVNLNSLATC TESNLVFGHV RASTQGVLAE TNCHPFSYGK IMFMHNGGIS
     AFDKIKKTII NYIEDKFFLL IQGSTDSECC FVLFLDTLYK MGYDPSDASV RFNHQVLRQA
     LLTTIELIKN WQVAITSEPS LLNFAVTDGE SVVVSRYITS KTDEAASLNF STGSRFFEYA
     PGRFKMERLD RAQDVIFVAS EPLTFERNDW MNVPTNTTIT ISKTNSVLMH PIMDEFYDSD
     GHERSSALAL SKGLIGGVPK PESDSDIDND SHINLTHEPL TQMTGKVY
//
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