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Database: UniProt/TrEMBL
Entry: E6VEJ9_RHOPX
LinkDB: E6VEJ9_RHOPX
Original site: E6VEJ9_RHOPX 
ID   E6VEJ9_RHOPX            Unreviewed;       424 AA.
AC   E6VEJ9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   28-MAR-2018, entry version 35.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ADU44031.1};
GN   OrderedLocusNames=Rpdx1_2440 {ECO:0000313|EMBL:ADU44031.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU44031.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Misra M., Chertkov O., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Logan B., Oda Y., Harwood C., Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) 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; CP002418; ADU44031.1; -; Genomic_DNA.
DR   RefSeq; WP_013502159.1; NC_014834.1.
DR   ProteinModelPortal; E6VEJ9; -.
DR   STRING; 652103.Rpdx1_2440; -.
DR   EnsemblBacteria; ADU44031; ADU44031; Rpdx1_2440.
DR   KEGG; rpx:Rpdx1_2440; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; GMTTQIY; -.
DR   OrthoDB; POG091H0APS; -.
DR   BioCyc; RPAL652103:G1GPO-2426-MONOMER; -.
DR   Proteomes; UP000001402; 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:ADU44031.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001402};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ADU44031.1}.
SQ   SEQUENCE   424 AA;  44574 MW;  ECC9FAABE9D66DF4 CRC64;
     MTNSELLTRR QAAVVRGVSQ ATPVFAERAL NSEIWDVEGK RYVDFAGGIA VLNTGHCHPH
     VVAAIRAQLD RFTHTCFQVS PYEGYIRLAE RLNELAPING PLKSILLSTG AEATENAVKI
     ARAATGRAGV IAFTGGFHGR TAFASAMTGK VIPYKKALGP PLPGVWHVPF PAAGGDVSVE
     DALRCVSFVF KADIDASQVA AIIIEPVQGE GGFHQAPPEL MRGLRRLCDE NGIVLIADEV
     QTGFGRTGKM FAMEHYDVQA DIVCVAKSLA GGLPLSGVIG RAAIMDAAEP GGLGGTYAGN
     PLACAAALAV LDVFEQENLI ARANQIGDRL RAAIDRFALS NTLVPTSPAR GPGAMVAFDI
     LKQRGGNEPD AETTKRVTQL AHENGLILLS CGTAANTIRI LVPLTASDAI VDEGLAILER
     CLAA
//
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