(data stored in ACNUC7421 zone)

SWISSPROT: A1AYR0_PARDP

ID   A1AYR0_PARDP            Unreviewed;       456 AA.
AC   A1AYR0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABL68404.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ABL68404.1};
GN   OrderedLocusNames=Pden_0290 {ECO:0000313|EMBL:ABL68404.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68404.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-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; CP000489; ABL68404.1; -; Genomic_DNA.
DR   RefSeq; WP_011746637.1; NC_008686.1.
DR   STRING; 318586.Pden_0290; -.
DR   PRIDE; A1AYR0; -.
DR   EnsemblBacteria; ABL68404; ABL68404; Pden_0290.
DR   KEGG; pde:Pden_0290; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   KO; K15785; -.
DR   OMA; SGHPICA; -.
DR   BioCyc; PDEN318586:G1GW1-283-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; -; 1.
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; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AYR0.
DR   SWISS-2DPAGE; A1AYR0.
KW   Aminotransferase {ECO:0000313|EMBL:ABL68404.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000313|EMBL:ABL68404.1}.
SQ   SEQUENCE   456 AA;  49183 MW;  EA023A3489CFF1CB CRC64;
     MLTNDELSKW DRESLFHPST NLGQFARGEG PQRIVSGAEG VYVTDRDGNR LLDGFAGLYC
     VNVGYGRPEI AEAIATQARE LAYYHAYAGH GSEASITLAK MVMDRAPRHM ARVYFGLGGS
     DANETNVKLV WYYNNIRGLP QKKKIISRWR GYHGSGLMTG SLTGLELFHK KFDLPLAQVI
     HTEAPYYYRR KDAGMSEEQF SAHCADELEK LIAAEGADTI AAFIGEPVLG TGGIVPPPKG
     YWEAIQKVLA RHDILLIADE VVTGFGRLGS MFGSDHYGMT PDIITCAKGL TSAYAPLSGS
     IVGQKVWEVL MQGTDEYGVL GHGWTYSAHP IGAAAGIANL RLIDELGLVG NAGRVGRYLN
     DRMRAAVGDH PNVGEIRGEG MLCAVELVRD RDTRGFFDAA EGIGGKVVGA MLKRGVIARA
     MPQGDIVGLA PPLCLTEAEA DVIVDVTAVA LRETLG
//

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