(data stored in SCRATCH zone)

SWISSPROT: Q13R45_PARXL

ID   Q13R45_PARXL            Unreviewed;       476 AA.
AC   Q13R45;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000256|HAMAP-Rule:MF_00423};
GN   ORFNames=Bxe_B2549 {ECO:0000313|EMBL:ABE33444.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33444.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33444.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33444.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00423, ECO:0000256|SAAS:SAAS00695329}.
CC   -!- CATALYTIC ACTIVITY: L-seryl-tRNA(Sec) + selenophosphate = L-
CC       selenocysteinyl-tRNA(Sec) + phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00423, ECO:0000256|SAAS:SAAS00695323}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00423,
CC         ECO:0000256|PIRSR:PIRSR618319-50,
CC         ECO:0000256|SAAS:SAAS00352468};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00423,
CC       ECO:0000256|SAAS:SAAS00695321}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423,
CC       ECO:0000256|SAAS:SAAS00695325}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00423, ECO:0000256|SAAS:SAAS00546326}.
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DR   EMBL; CP000271; ABE33444.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_B2549; -.
DR   EnsemblBacteria; ABE33444; ABE33444; Bxe_B2549.
DR   KEGG; bxb:DR64_4875; -.
DR   KEGG; bxe:Bxe_B2549; -.
DR   eggNOG; ENOG4105C1Y; Bacteria.
DR   eggNOG; COG1921; LUCA.
DR   HOGENOM; HOG000163726; -.
DR   KO; K01042; -.
DR   OMA; LESFCVK; -.
DR   OrthoDB; POG091H06BG; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_00423; SelA; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR018319; SelA-like.
DR   InterPro; IPR004534; SelA_trans.
DR   InterPro; IPR025862; SelA_trans_N_dom.
DR   PANTHER; PTHR32328:SF2; PTHR32328:SF2; 1.
DR   Pfam; PF12390; Se-cys_synth_N; 1.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00474; selA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13R45.
DR   SWISS-2DPAGE; Q13R45.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423,
KW   ECO:0000256|SAAS:SAAS00695320};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00423,
KW   ECO:0000256|SAAS:SAAS00695331};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00423,
KW   ECO:0000256|PIRSR:PIRSR618319-50, ECO:0000256|SAAS:SAAS00029257};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Selenium {ECO:0000256|HAMAP-Rule:MF_00423,
KW   ECO:0000256|SAAS:SAAS00695335};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00423,
KW   ECO:0000256|SAAS:SAAS00695324, ECO:0000313|EMBL:ABE33444.1}.
FT   DOMAIN       15     52       Se-cys_synth_N. {ECO:0000259|Pfam:
FT                                PF12390}.
FT   MOD_RES     301    301       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00423,
FT                                ECO:0000256|PIRSR:PIRSR618319-50}.
SQ   SEQUENCE   476 AA;  51042 MW;  A0A22005471F6033 CRC64;
     MSDVSGSELR ALMARVPSVE KVMASAEFTP LIGEYGRTQV LGAVREALDN WRTSAQSGAA
     SVSALDAAQL KDSVEATLRQ RNQSRLRSVF NLTGTVLHTN LGRALLPDEA VQSVMKALTQ
     PANLEFDLDT GKRGDRDDLI DELICELTGA EAATVVNNNA AAVLLALSAL ASKKEVIVSR
     GELVEIGGAF RIPDIMSRAG ARLREVGTTN RTHLKDYEEA IGPQTALLMK VHASNYAING
     FTKEVGLDEI APLAHARGLA VAVDLGSGTL VDLGQWGLPR EPTVRETVKA GADLVTFSGD
     KLLGGPQAGL IVGRRDLIAK IKKHPLKRAL RVGKLTLAAL EPVLQLYRAP EKLTERLTTL
     RLLTRPADDI RLAAERVQPA LQRALGERYA VAAEPMFSQI GSGALPVDVL PSYGLVVRTA
     DGKRGGRQLL ALEKLLREMA RPVIGRIADD ALRLDLRCLE AADEAQLIGQ LEGVRA
//

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