(data stored in SCRATCH zone)

SWISSPROT: Q3IFU1_PSEHT

ID   Q3IFU1_PSEHT            Unreviewed;       193 AA.
AC   Q3IFU1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 74.
DE   SubName: Full=Putative glutamine amidotransferase putatively involved in paraminobenzoate biosynthesis {ECO:0000313|EMBL:CAI85295.1};
DE            EC=4.1.3.27 {ECO:0000313|EMBL:CAI85295.1};
GN   Name=pabA {ECO:0000313|EMBL:CAI85295.1};
GN   OrderedLocusNames=PSHAa0192 {ECO:0000313|EMBL:CAI85295.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85295.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85295.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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DR   EMBL; CR954246; CAI85295.1; -; Genomic_DNA.
DR   RefSeq; WP_011326910.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFU1; -.
DR   STRING; 326442.PSHAa0192; -.
DR   MEROPS; C26.955; -.
DR   EnsemblBacteria; CAI85295; CAI85295; PSHAa0192.
DR   GeneID; 32566248; -.
DR   KEGG; pha:PSHAa0192; -.
DR   eggNOG; ENOG4105DDQ; Bacteria.
DR   eggNOG; COG0512; LUCA.
DR   HOGENOM; HOG000025029; -.
DR   KO; K01664; -.
DR   OMA; APELMHG; -.
DR   OrthoDB; POG091H01Q6; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
DR   PRODOM; Q3IFU1.
DR   SWISS-2DPAGE; Q3IFU1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Glutamine amidotransferase {ECO:0000313|EMBL:CAI85295.1};
KW   Lyase {ECO:0000313|EMBL:CAI85295.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000313|EMBL:CAI85295.1}.
FT   DOMAIN        1    193       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
SQ   SEQUENCE   193 AA;  21595 MW;  27301A4A105BA9E1 CRC64;
     MLLMIDNYDS FTYNLVQYFQ RLDQEVLVKR NDQITLSQIK QLNPQHIVIS PGPKSPSEAG
     ISLSIVEQLK GQYPILGICL GHQTIAQALG AKVVRAKKVM HGKTSPIYHS DQGVFKGLAK
     PLTVCRYHSL IVEAQSLPKE LQVTAWTQTQ QGEFDEIMGL LHTDLALEGV QFHPEAILTE
     QGLALLDNFL TRF
//

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