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SALL_METJA
ID   SALL_METJA              Reviewed;         263 AA.
AC   Q59045;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Chlorinase MJ1651;
DE            EC=2.5.1.-;
GN   OrderedLocusNames=MJ1651;
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 (2.5 ANGSTROMS) OF 2-261, AND SUBUNIT.
RX   PubMed=17910070; DOI=10.1002/prot.21646;
RA   Rao K.N., Burley S.K., Swaminathan S.;
RT   "Crystal structure of a conserved protein of unknown function (MJ1651) from
RT   Methanococcus jannaschii.";
RL   Proteins 70:572-577(2008).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17910070}.
CC   -!- SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase
CC       family. {ECO:0000305}.
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DR   EMBL; L77117; AAB99672.1; -; Genomic_DNA.
DR   PIR; A64506; A64506.
DR   PDB; 2F4N; X-ray; 2.50 A; A/B/C=2-261.
DR   PDBsum; 2F4N; -.
DR   AlphaFoldDB; Q59045; -.
DR   SMR; Q59045; -.
DR   STRING; 243232.MJ_1651; -.
DR   PRIDE; Q59045; -.
DR   EnsemblBacteria; AAB99672; AAB99672; MJ_1651.
DR   KEGG; mja:MJ_1651; -.
DR   eggNOG; arCOG04309; Archaea.
DR   HOGENOM; CLU_059734_1_1_2; -.
DR   InParanoid; Q59045; -.
DR   OMA; EGYVGAM; -.
DR   PhylomeDB; Q59045; -.
DR   EvolutionaryTrace; Q59045; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.90; -; 1.
DR   Gene3D; 3.40.50.10790; -; 1.
DR   InterPro; IPR002747; SAM_Chlor/Fluor.
DR   InterPro; IPR023227; SAM_OH_AdoTrfase_C.
DR   InterPro; IPR023228; SAM_OH_AdoTrfase_N.
DR   PANTHER; PTHR35092; PTHR35092; 1.
DR   Pfam; PF01887; SAM_adeno_trans; 1.
DR   PIRSF; PIRSF006779; UCP006779; 1.
DR   SUPFAM; SSF101852; SSF101852; 1.
DR   SUPFAM; SSF102522; SSF102522; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Transferase.
FT   CHAIN           1..263
FT                   /note="Chlorinase MJ1651"
FT                   /id="PRO_0000107459"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           25..38
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          45..51
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          101..108
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           111..117
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           139..152
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   TURN            223..226
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   HELIX           247..251
FT                   /evidence="ECO:0007829|PDB:2F4N"
FT   STRAND          258..261
FT                   /evidence="ECO:0007829|PDB:2F4N"
SQ   SEQUENCE   263 AA;  30249 MW;  801E2C3E5A66CDD0 CRC64;
     MGIYMRDDIL DIITLTTDFG TNEGYVGAMK GRILNILKKY NKDAKIIDIS HEIKPFNIYH
     GAYVLLTAIP YFPPSVHVAV IDPTVGSERK SIVIETKSGY YLVGPDNGLF TYVAEKLGIK
     RIIKIDEERY KPSSTFHGRD VYAVVGAEIL INNGYDGEEL DEMVKIDETK KRVIHIDRFG
     NIITNIKKDE VTFKYYDTIM IKIRHKNGIE KIIKCKFVKS YFEEKNNFIC LINSEGFLEI
     SKFMDNASKL LNVDYLDEIE IIY
 
 
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