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Database: UniProt
Entry: Q8ZUE9
LinkDB: Q8ZUE9
Original site: Q8ZUE9 
ID   PDXT_PYRAE              Reviewed;         204 AA.
AC   Q8ZUE9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   01-OCT-2014, entry version 61.
DE   RecName: Full=Glutamine amidotransferase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
DE            EC=2.6.-.- {ECO:0000255|HAMAP-Rule:MF_01615};
DE   AltName: Full=Glutamine amidotransferase glutaminase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
GN   Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615};
GN   OrderedLocusNames=PAE2820;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630
OS   / NBRC 100827).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- FUNCTION: Involved in the hydrolysis of glutamine to glutamate and
CC       ammonia. Channels an ammonia molecule to PdxS. {ECO:0000255|HAMAP-
CC       Rule:MF_01615}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01615}.
CC   -!- SUBUNIT: Forms a complex with PdxS. {ECO:0000255|HAMAP-
CC       Rule:MF_01615}.
CC   -!- SIMILARITY: Belongs to the glutamine amidotransferase PdxT/SNO
CC       family. {ECO:0000255|HAMAP-Rule:MF_01615}.
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DR   EMBL; AE009441; AAL64458.1; -; Genomic_DNA.
DR   RefSeq; NP_560276.1; NC_003364.1.
DR   ProteinModelPortal; Q8ZUE9; -.
DR   STRING; 178306.PAE2820; -.
DR   EnsemblBacteria; AAL64458; AAL64458; PAE2820.
DR   GeneID; 1463620; -.
DR   KEGG; pai:PAE2820; -.
DR   eggNOG; COG0311; -.
DR   HOGENOM; HOG000039949; -.
DR   KO; K08681; -.
DR   OMA; RKINCIP; -.
DR   BioCyc; PAER178306:GCEO-2027-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01615; PdxT; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR021196; PdxT/SNO_CS.
DR   InterPro; IPR002161; PDXT_SNO_fam.
DR   Pfam; PF01174; SNO; 1.
DR   PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1.
DR   PROSITE; PS01236; PDXT_SNO_1; 1.
DR   PROSITE; PS51130; PDXT_SNO_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glutamine amidotransferase; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN         1    204       Glutamine amidotransferase subunit PdxT.
FT                                /FTId=PRO_0000135687.
FT   ACT_SITE     84     84       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01615}.
FT   ACT_SITE    184    184       {ECO:0000255|HAMAP-Rule:MF_01615}.
FT   ACT_SITE    186    186       {ECO:0000255|HAMAP-Rule:MF_01615}.
FT   BINDING     116    116       Glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01615}.
SQ   SEQUENCE   204 AA;  21560 MW;  38D855EA04D4407A CRC64;
     MKIGVLALQG DVEEHANAFK EAGREVGVDV DVVEVKKPGD LKDIKALAIP GGESTTIGRL
     AKRTGLLDAV KKAIEGGVPA LGTCAGAIFM AKEVKDAVVG ATGQPVLGVM DIAVVRNAFG
     RQRESFEAEV VLENLGKLKA VFIRAPAFVR AWGSAKLLAP LRHNQLGLVY AAAVQNNMVA
     TAFHPELTTT AVHKWVINMA LGRF
//
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