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Database: UniProt/TrEMBL
Entry: G2NMA8_STREK
LinkDB: G2NMA8_STREK
Original site: G2NMA8_STREK 
ID   G2NMA8_STREK            Unreviewed;       446 AA.
AC   G2NMA8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-FEB-2018, entry version 37.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEN12686.1};
GN   ORFNames=SACTE_4860 {ECO:0000313|EMBL:AEN12686.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12686.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN12686.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) 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; CP002993; AEN12686.1; -; Genomic_DNA.
DR   RefSeq; WP_014048637.1; NC_015953.1.
DR   ProteinModelPortal; G2NMA8; -.
DR   STRING; 862751.SACTE_4860; -.
DR   EnsemblBacteria; AEN12686; AEN12686; SACTE_4860.
DR   KEGG; ssx:SACTE_4860; -.
DR   PATRIC; fig|862751.12.peg.5038; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   KO; K07250; -.
DR   OrthoDB; POG091H0APS; -.
DR   BioCyc; SSP862751:G1GPM-4931-MONOMER; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; -; 2.
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; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AEN12686.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001397};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   Transferase {ECO:0000313|EMBL:AEN12686.1}.
SQ   SEQUENCE   446 AA;  46709 MW;  262FF27114F442A4 CRC64;
     MSDIPQERRV LTAIPGPKSV ELQARRTAAV AAGVGSTLPV FTARAGGGII EDVDGNRLID
     FGSGIAVTSV GASAEAVVRR ASAQLADFTH TCFMVTPYEG YVEVCERLAE LTPGDHAKKS
     ALFNSGAEAV ENAVKIARAY TKRTAVVVFD HGYHGRTNLT MALTSKNMPY KQGFGPFAPE
     VYRVPVAYGY RWPTGPENAG AEASAQAIDE ITKQIGAENV AAIIIEPVLG EGGFIEPAKG
     FLPAIARFAK DNGIVFVADE IQSGFCRTGQ WFACEDEGIV PDLITTAKGI AGGLPLSAVT
     GRAEIMDAAH SGGLGGTYGG NPVACAGALG AIETMRELDL NARARRIEEV MKGRLEEMRA
     KLPNGGVIGD VRGRGAMIAI ELVKPGTKDP DAAATAALAK ACHAEGLLVL TCGTYGNVLR
     FLPPLVIGED LLNEGLDILE RAFATL
//
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