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Database: UniProt/TrEMBL
Entry: Q0RYH2_RHOJR
LinkDB: Q0RYH2_RHOJR
Original site: Q0RYH2_RHOJR 
ID   Q0RYH2_RHOJR            Unreviewed;       438 AA.
AC   Q0RYH2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:ABG99664.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABG99664.1};
GN   OrderedLocusNames=RHA1_ro08620 {ECO:0000313|EMBL:ABG99664.1};
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL1 {ECO:0000313|EMBL:ABG99664.1,
OG   ECO:0000313|Proteomes:UP000008710}.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG99664.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RC   PLASMID=Plasmid pRHL1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000432; ABG99664.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0RYH2; -.
DR   PRIDE; Q0RYH2; -.
DR   EnsemblBacteria; ABG99664; ABG99664; RHA1_ro08620.
DR   KEGG; rha:RHA1_ro08620; -.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0ER2; -.
DR   BioCyc; RJOS101510:GJJ1-7894-MONOMER; -.
DR   Proteomes; UP000008710; Plasmid pRHL1.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABG99664.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Plasmid {ECO:0000313|EMBL:ABG99664.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000313|EMBL:ABG99664.1}.
SQ   SEQUENCE   438 AA;  46766 MW;  29884D1C02C65E63 CRC64;
     MNDVSLHQRH RAVMPDWLST YYEDNPLELV SGSGRHVTGG DGRTYLDFFG GLLATMIGHD
     IPEITEALRR QAGQLLHSST LYLIRSQVEL AEKIAARAPV DNPRVFFVNS GSEAVETALL
     LTTTAQQSNQ VIALRGSYHG RSFGTVATTG IRGWSATSLS PLQVTYAHSG YKYRSPFGHL
     DDHAFNTACR DELQTMIETS TSGNIACYLA EPIQGAGGFA TPPDGFFLAM KEVLDAYDIP
     FVSDEVQSGW GRTGRSYFGI EHYGVRPEAI TFAKGLANGL SIGGVVAENE LMNCLTANSI
     STAGGNPIAM AAGNAVLDFI ESHDLQANAA DVGHLLSTGL QELATRHPLI GDVRGAGLML
     GVELVENGTK KPAVAATNTI LTQCRERGLL IGKGGLSGNV LRVTPPMTVT IEEAKQALGI
     LDDVLSYVAS RAEPQPIH
//
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