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Database: UniProt/TrEMBL
Entry: Q1AZI0_RUBXD
LinkDB: Q1AZI0_RUBXD
Original site: Q1AZI0_RUBXD 
ID   Q1AZI0_RUBXD            Unreviewed;       436 AA.
AC   Q1AZI0;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   07-JUN-2017, entry version 70.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABG03198.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ABG03198.1};
GN   OrderedLocusNames=Rxyl_0220 {ECO:0000313|EMBL:ABG03198.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales;
OC   Rubrobacteraceae; Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG03198.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG03198.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E.,
RA   Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000386; ABG03198.1; -; Genomic_DNA.
DR   RefSeq; WP_011563216.1; NC_008148.1.
DR   ProteinModelPortal; Q1AZI0; -.
DR   STRING; 266117.Rxyl_0220; -.
DR   EnsemblBacteria; ABG03198; ABG03198; Rxyl_0220.
DR   KEGG; rxy:Rxyl_0220; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0ER2; -.
DR   BioCyc; RXYL266117:GH8O-221-MONOMER; -.
DR   Proteomes; UP000006637; 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;
KW   Aminotransferase {ECO:0000313|EMBL:ABG03198.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006637};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006637};
KW   Transferase {ECO:0000313|EMBL:ABG03198.1}.
SQ   SEQUENCE   436 AA;  46949 MW;  6624511794AFA5ED CRC64;
     MRPGELHERH RAALPAWLSL YYERPIELVR GEGFRVWDSE GNEYLDFFGG IVTTISGHAV
     PEIVEAVKEQ AERILHSSTL YLIESQVRLA EKLISLSPIS GEQKVFFVGS GSEANEAALL
     FATQYRGSSE VIALRGSYHG GSFGTMGITG QSSWRPTPRT ALDVSYAMPP HRSYSPLYGR
     FGDPEELARA CAEDVRSLIE TSTTGRVAAF IAEPIQGVGG FIELPPAYLS RVKEILEEHG
     VLFVSDEVQT AFGRTGSHFW GIERSGVEPD LITMAKGLGN GLAIGAVMGR AEVIDSLSPK
     LHISTFGGNP VSTAGALANL EYILENDLQR NAEEVGSYLK ERLLGLAAEH ASVGEVRGRG
     LMLAVELVRE GAPDPQAAAA FMEACRERGV LVGKGGLKGN AIRISPPLTV TREAAEEAAR
     VFDEALSSVE AGERVV
//
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