(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZKM9_PSEAB

ID   A0A0H2ZKM9_PSEAB        Unreviewed;       456 AA.
AC   A0A0H2ZKM9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   SubName: Full=Putrescine aminotransferase {ECO:0000313|EMBL:ABJ15261.1};
GN   Name=spuC {ECO:0000313|EMBL:ABJ15261.1};
GN   OrderedLocusNames=PA14_03900 {ECO:0000313|EMBL:ABJ15261.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15261.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15261.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15261.1,
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; ABJ15261.1; -; Genomic_DNA.
DR   RefSeq; WP_003084297.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKM9; -.
DR   SMR; A0A0H2ZKM9; -.
DR   EnsemblBacteria; ABJ15261; ABJ15261; PA14_03900.
DR   KEGG; pau:PA14_03900; -.
DR   KO; K12256; -.
DR   OMA; VWSYAHP; -.
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; A0A0H2ZKM9.
DR   SWISS-2DPAGE; A0A0H2ZKM9.
KW   Aminotransferase {ECO:0000313|EMBL:ABJ15261.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABJ15261.1}.
SQ   SEQUENCE   456 AA;  50453 MW;  01493131BE1683B8 CRC64;
     MNSQITNAKT REWQALSRDH HLPPFTDYKQ LNEKGARIIT KAEGVYIWDS EGNKILDAMA
     GLWCVNVGYG REELVQAATR QMRELPFYNL FFQTAHPPVV ELAKAIADVA PEGMNHVFFT
     GSGSEANDTV LRMVRHYWAT KGQPQKKVVI GRWNGYHGST VAGVSLGGMK ALHEQGDFPI
     PGIVHIAQPY WYGEGGDMSP DEFGVWAAEQ LEKKILEVGE ENVAAFIAEP IQGAGGVIVP
     PDTYWPKIRE ILAKYDILFI ADEVICGFGR TGEWFGSQYY GNAPDLMPIA KGLTSGYIPM
     GGVVVRDEIV EVLNQGGEFY HGFTYSGHPV AAAVALENIR ILREEKIIEK VKAETAPYLQ
     KRWQELADHP LVGEARGVGM VAALELVKNK KTRERFTDKG VGMLCREHCF RNGLIMRAVG
     DTMIISPPLV IDPSQIDELI TLARKCLDQT AAAVLA
//

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