SELA_AQUAE
ID SELA_AQUAE Reviewed; 452 AA.
AC O67140;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423};
DE EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423};
GN Name=selA {ECO:0000255|HAMAP-Rule:MF_00423}; OrderedLocusNames=aq_1031;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00423}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00423};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00423};
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:0000255|HAMAP-Rule:MF_00423}.
CC -!- INTERACTION:
CC O67140; O67140: selA; NbExp=3; IntAct=EBI-16044058, EBI-16044058;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC Rule:MF_00423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC07094.1; -; Genomic_DNA.
DR PIR; A70389; A70389.
DR RefSeq; NP_213703.1; NC_000918.1.
DR RefSeq; WP_010880641.1; NC_000918.1.
DR PDB; 3W1H; X-ray; 3.89 A; A/B/C/D/E=1-452.
DR PDB; 3W1I; X-ray; 3.19 A; A/B/C/D/E/F/G/H/I/J=62-452.
DR PDB; 3W1J; X-ray; 3.25 A; A/B/C/D/E/F/G/H/I/J=62-452.
DR PDB; 3W1K; X-ray; 7.50 A; A/B/C/D/E=1-452.
DR PDB; 3WCN; X-ray; 3.35 A; A/B=1-452.
DR PDB; 3WCO; X-ray; 2.40 A; A/B=62-452.
DR PDBsum; 3W1H; -.
DR PDBsum; 3W1I; -.
DR PDBsum; 3W1J; -.
DR PDBsum; 3W1K; -.
DR PDBsum; 3WCN; -.
DR PDBsum; 3WCO; -.
DR AlphaFoldDB; O67140; -.
DR SMR; O67140; -.
DR DIP; DIP-61414N; -.
DR STRING; 224324.aq_1031; -.
DR PRIDE; O67140; -.
DR EnsemblBacteria; AAC07094; AAC07094; aq_1031.
DR KEGG; aae:aq_1031; -.
DR PATRIC; fig|224324.8.peg.805; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_0; -.
DR InParanoid; O67140; -.
DR OMA; GATNRTH; -.
DR OrthoDB; 1124266at2; -.
DR BRENDA; 2.9.1.1; 396.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central.
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.
DR InterPro; IPR018319; SelA-like.
DR InterPro; IPR004534; SelA_trans.
DR Pfam; PF03841; SelA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00474; selA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Selenium; Transferase.
FT CHAIN 1..452
FT /note="L-seryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000189594"
FT MOD_RES 285
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:3WCN"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:3WCN"
FT HELIX 24..43
FT /evidence="ECO:0007829|PDB:3WCN"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:3WCN"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3WCO"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3WCO"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3W1I"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3WCO"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3W1J"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3W1I"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 318..332
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:3WCO"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:3W1I"
FT STRAND 390..402
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 404..413
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:3WCO"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3W1I"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:3WCO"
FT HELIX 439..449
FT /evidence="ECO:0007829|PDB:3WCO"
SQ SEQUENCE 452 AA; 50848 MW; E511326E17E9F015 CRC64;
MKSLLRQIPQ ISKVVEIFKK KYPEIYVVKA AREVAEKYRK EIIEGKRKDL NGFLEDVERK
IKSLMKPNIK RVINATGVVI NTNLGRAPLS KDVINFISEI ANGYSNLEYN LEEGKRGSRI
AHIEKYLNEL TGAESSFVVN NNAGAVFLVL NTLAEGKEVI ISRGELVEIG GSFRIPDIMK
KSGAILREVG TTNKTKVSDY EGAINQNTAL LMKVHKSNFY MEGFVEEVKL EDLVKLGHKY
GIPTYYDAGS GLLINLKEFG ISVDEPNFRD CISLGIDLVS GSGDKLLGGP QAGIIVGKKN
LIEKIKKNPI ARALRIDKLT LSGLEMTLKL YFEKRYEDIP VIRMLTQDEK ALRQKAKRLE
KLLKDIPGLK ISVIKDKAKP GGGSLPELEL PTYCVAIRHD RLSSQELSRR LRLAEPPIVC
RIREDQLLFD MRTVFHEDLK TIKKTLQELL SI
