(data stored in SCRATCH zone)

SWISSPROT: Q3KJX4_PSEPF

ID   Q3KJX4_PSEPF            Unreviewed;       425 AA.
AC   Q3KJX4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABA71932.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABA71932.1};
GN   OrderedLocusNames=Pfl01_0188 {ECO:0000313|EMBL:ABA71932.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71932.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71932.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71932.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000094; ABA71932.1; -; Genomic_DNA.
DR   RefSeq; WP_011331899.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0188; -.
DR   World-2DPAGE; 0008:Q3KJX4; -.
DR   PRIDE; Q3KJX4; -.
DR   EnsemblBacteria; ABA71932; ABA71932; Pfl01_0188.
DR   KEGG; pfo:Pfl01_0188; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K14268; -.
DR   OMA; VNNVGHC; -.
DR   BioCyc; PFLU205922:G1G4S-191-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJX4.
DR   SWISS-2DPAGE; Q3KJX4.
KW   Aminotransferase {ECO:0000313|EMBL:ABA71932.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABA71932.1}.
SQ   SEQUENCE   425 AA;  44826 MW;  401F78073C37D0F5 CRC64;
     MSKTNAELMA RRTAAVPRGV GQIHPIFAES AKNATVTDVE GREFIDFAGG IAVLNTGHVH
     PKIIAAVTEQ LNKLTHTCFQ VLAYEPYVEL CEKINARVPG DFAKKTLLVT TGSEAVENAV
     KIARAATGRA GVIAFTGAYH GRTMMTLGLT GKVVPYSAGM GLMPGGIFRA LYPNELHGVS
     IDDSIASIER IFKNDAEPKD IAAIIIEPVQ GEGGFYVAPK EFMKRLRALC DQHGILLIAD
     EVQTGAGRTG TFFAMEQMGV AADLTTFAKS IAGGFPLAGV CGKAEYMDAI APGGLGGTYA
     GSPIACAAAL AVMEVFEEEK LLDRCKAVGE RLVTGLKAIQ AKHPVIGEVR ALGAMIAVEL
     FENGDSHKPN PTAVAAVVAK ARDKGLILLS CGTYGNVLRV LVPLTSPDEQ LDKGLAIIEE
     CFSEL
//

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