Y158_METJA
ID Y158_METJA Reviewed; 374 AA.
AC Q57622;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=UPF0425 pyridoxal phosphate-dependent protein MJ0158;
GN OrderedLocusNames=MJ0158;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH
RP COFACTOR, SUBUNIT, MASS SPECTROMETRY, AND PYRIDOXAL PHOSPHATE AT LYS-208.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=16201757; DOI=10.1021/bi051110r;
RA Kaiser J.T., Gromadski K., Rother M., Engelhardt H., Rodnina M.V.,
RA Wahl M.C.;
RT "Structural and functional investigation of a putative archaeal
RT selenocysteine synthase.";
RL Biochemistry 44:13315-13327(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16201757}.
CC -!- MASS SPECTROMETRY: Mass=41886; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:16201757};
CC -!- MASS SPECTROMETRY: Mass=42114; Method=Unknown; Note=The measured mass
CC is that of the PLP-bound protein.;
CC Evidence={ECO:0000269|PubMed:16201757};
CC -!- SIMILARITY: Belongs to the UPF0425 family. {ECO:0000305}.
CC -!- CAUTION: Despite a certain similarity to SelA, PubMed:16201757 reported
CC that this protein does not harbor SelA activity, i.e. it fails to bind
CC to Ser-tRNA(Sec) and is not able to convert this substrate to
CC selenocysteinyl-tRNA(Sec). It also does not convert O-phosphoseryl-
CC tRNA(Sec) to selenocysteinyl-tRNA(Sec). {ECO:0000305}.
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DR EMBL; L77117; AAB98142.1; -; Genomic_DNA.
DR PIR; G64319; G64319.
DR RefSeq; WP_010869653.1; NC_000909.1.
DR PDB; 2AEU; X-ray; 1.70 A; A=1-374.
DR PDB; 2AEV; X-ray; 2.00 A; A=1-374.
DR PDBsum; 2AEU; -.
DR PDBsum; 2AEV; -.
DR AlphaFoldDB; Q57622; -.
DR SMR; Q57622; -.
DR STRING; 243232.MJ_0158; -.
DR EnsemblBacteria; AAB98142; AAB98142; MJ_0158.
DR GeneID; 1451005; -.
DR KEGG; mja:MJ_0158; -.
DR eggNOG; arCOG00114; Archaea.
DR HOGENOM; CLU_055443_0_0_2; -.
DR InParanoid; Q57622; -.
DR OMA; RIDFCSK; -.
DR OrthoDB; 37272at2157; -.
DR PhylomeDB; Q57622; -.
DR EvolutionaryTrace; Q57622; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR020033; PyrdxlP-dep_transferase_arc.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR018319; SelA-like.
DR Pfam; PF03841; SelA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03576; pyridox_MJ0158; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..374
FT /note="UPF0425 pyridoxal phosphate-dependent protein
FT MJ0158"
FT /id="PRO_0000106722"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:2AEU"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:2AEU"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 296..307
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 308..326
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2AEV"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2AEU"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:2AEU"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:2AEU"
SQ SEQUENCE 374 AA; 41880 MW; 3ED87DC642AA0AB8 CRC64;
MLSDYEEFLR LEKARKIILE ILNEKGRDAL YDLSGLSGGF LIDEKDKALL NTYIGSSYFA
EKVNEYGLKH LGGDENDKCV GFNRTSSAIL ATILALKPKK VIHYLPELPG HPSIERSCKI
VNAKYFESDK VGEILNKIDK DTLVIITGST MDLKVIELEN FKKVINTAKN KEAIVFVDDA
SGARVRLLFN QPPALKLGAD LVVTSTDKLM EGPRGGLLAG KKELVDKIYI EGTKFGLEAQ
PPLLAGIYRA LKNFNLERIR KAFERAKNFD LSKIEKLNKE LKAIDDNINI VYERTPTGFV
IKRVYKDDTI NIKKLIEIGF NLLKNYGIIT ITVAGMPGAS KSLRIDLTSR DAERIDDNYI
IKAIVESIKM AFKS
