(data stored in SCRATCH zone)

SWISSPROT: B2JM22_PARP8

ID   B2JM22_PARP8            Unreviewed;       478 AA.
AC   B2JM22;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACC72712.1};
GN   OrderedLocusNames=Bphy_3573 {ECO:0000313|EMBL:ACC72712.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72712.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001044; ACC72712.1; -; Genomic_DNA.
DR   RefSeq; WP_012402885.1; NC_010623.1.
DR   STRING; 391038.Bphy_3573; -.
DR   EnsemblBacteria; ACC72712; ACC72712; Bphy_3573.
DR   GeneID; 27743243; -.
DR   KEGG; bph:Bphy_3573; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   KO; K12256; -.
DR   OMA; AHKVPNT; -.
DR   OrthoDB; 478143at2; -.
DR   BioCyc; BPHY391038:G1GBS-3669-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
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; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JM22.
DR   SWISS-2DPAGE; B2JM22.
KW   Aminotransferase {ECO:0000313|EMBL:ACC72712.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000313|EMBL:ACC72712.1}.
SQ   SEQUENCE   478 AA;  52299 MW;  A335795E163698BC CRC64;
     MSFRTEEIAY AQPARPAATA STSQQQRSTA EYRALDAAHH IHPFSDMGAL NSAGSRVIVK
     AEGVYLWDSD GNKIIDGMAG LWCVNVGYGR KELADAAYQQ LRELPFYNTF FKTTHPPVIE
     LSALLAEVTP APFNHFFYCN SGSEGNDTVL RIVHQYWATQ SKKLKKFVIS RKNGYHGSTI
     AGGTLGGMGY MHEQMPSQVE HIVHIDQPYW FGEGGDMTPE EFGLARARQL EAEILELGAE
     NVAAFIGEPF QGAGGVIFPP STYWPEIQRI CRKYDVLLVA DEVIGGFGRT GEWFAHQHFG
     FEPDLITMAK GLTSGYIPMG AVGLHDRIAK AIIENGEFNH GLTYSGHPVA AAVAVANLKL
     LRDEKIVERV KNETGPYFQQ SLREAFASQP IVGEVAGTGL VAGIQLAENP KTRKRFENGG
     DVGTICRDFC FNGNLIMRAT GDRMLLSPPL VVTKSEIDEI VSKAKKAIDA TAQQLGLA
//

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