(data stored in ACNUC7421 zone)

SWISSPROT: Q13E06_RHOPS

ID   Q13E06_RHOPS            Unreviewed;       412 AA.
AC   Q13E06;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=RPD_0445 {ECO:0000313|EMBL:ABE37683.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37683.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37683.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37683.1,
RC   ECO:0000313|Proteomes:UP000001818};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP000283; ABE37683.1; -; Genomic_DNA.
DR   RefSeq; WP_011500871.1; NC_007958.1.
DR   STRING; 316057.RPD_0445; -.
DR   EnsemblBacteria; ABE37683; ABE37683; RPD_0445.
DR   KEGG; rpd:RPD_0445; -.
DR   eggNOG; ENOG4105CHM; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223059; -.
DR   OMA; EVLFNFP; -.
DR   OrthoDB; 417859at2; -.
DR   BioCyc; RPAL316057:RPD_RS02285-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E06.
DR   SWISS-2DPAGE; Q13E06.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ABE37683.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ABE37683.1}.
FT   DOMAIN       43    402       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   412 AA;  44072 MW;  C9E59B2A20513E39 CRC64;
     MALPASSASA RAAGSPSAAG HSERSPFARL TELLAPYQPG ERLINLSLGE PQHPVPDFVG
     PVLAQHIADF GRYPMAKGIA PFRNAAASWL AQRFALPRAP DPETEVLVLN GSREGLFLAA
     LAAARHVGPR DGTPAILMPN PFYPAYAAGA RAAGCEAVFL PTNLANGFLP DLESLDEATL
     KRTVAIYIAS PANPQGSVAS RDYFARLKAL ADRYGFLILA DECYSEIYTR TAPGSALEAA
     GPDFRNVAVF QSLSKRSNLP GMRVGFVAGD ADFLNAFHEL RNVAAPQVPV ALQHVAVAAY
     GDEAHVEENR RLYRLKFDLA DQILGERFGY QRPAGGFCLW LDVSAHGGDE AATVKLFREG
     GVRVIPGSYL ARPQPDGSNP GAGYIRLAMV QDSESTAEAL HRLVRILDES RG
//

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