(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZLL5_PSEAB

ID   A0A0H2ZLL5_PSEAB        Unreviewed;       393 AA.
AC   A0A0H2ZLL5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=Class III pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:ABJ15493.1};
GN   Name=argD {ECO:0000313|EMBL:ABJ15493.1};
GN   OrderedLocusNames=PA14_06920 {ECO:0000313|EMBL:ABJ15493.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15493.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15493.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15493.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000438; ABJ15493.1; -; Genomic_DNA.
DR   RefSeq; WP_003084899.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZLL5; -.
DR   SMR; A0A0H2ZLL5; -.
DR   EnsemblBacteria; ABJ15493; ABJ15493; PA14_06920.
DR   KEGG; pau:PA14_06920; -.
DR   KO; K00821; -.
DR   OMA; GNPLMTA; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZLL5.
DR   SWISS-2DPAGE; A0A0H2ZLL5.
KW   Aminotransferase {ECO:0000313|EMBL:ABJ15493.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABJ15493.1}.
SQ   SEQUENCE   393 AA;  41885 MW;  1A221122FC61095C CRC64;
     MADALDSLRL MRTQERPAQV FVRGQGSWLW DSDGRAFLDF TQGLAVNCLG HSPSVLVQAL
     ARQARELVSA GPGLLNRPVL ALAQRLCLAT GSDQAYFLTS GAEANEAAIA LARKWGRLHR
     GGAQRIVSTV NSIHGRTPGT LTACGKPAQH GLEGFARVPF NDLDAMAAAI DEETVAVMLE
     PVQGDAGVIP ATLDYLRGIE RLCRQRGVLL ILDEVQTGIG RCGALLAEEL YGVRADIVTL
     GKGLGAGVPL SALLARGNAC CFEPGDQLGT HHGNALMTAA GLAVLNTVLE PGFLEQVREQ
     GTHLRDGLAR VARRYGHGPL RGQGLFWGLP LIGQRAPAVV RAAFGEGLLI NAPQPHCLRF
     SPALTVSRAN VDEMLRRLER ALARVANRHE EVA
//

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