(data stored in ACNUC7421 zone)

SWISSPROT: SELO_PSEPF

ID   SELO_PSEPF              Reviewed;         487 AA.
AC   Q3KJ68;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=Protein adenylyltransferase SelO {ECO:0000255|HAMAP-Rule:MF_00692};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00692};
DE            EC=2.7.7.n1 {ECO:0000255|HAMAP-Rule:MF_00692};
GN   Name=selO {ECO:0000255|HAMAP-Rule:MF_00692}; OrderedLocusNames=Pfl01_0444;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC       Ser, Thr or Tyr residues of target proteins (AMPylation).
CC       {ECO:0000255|HAMAP-Rule:MF_00692}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC         [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54293;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein]
CC         + diphosphate; Xref=Rhea:RHEA:58120, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:15073, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:142516; Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58121;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- SIMILARITY: Belongs to the SELO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00692}.
DR   EMBL; CP000094; ABA72188.1; -; Genomic_DNA.
DR   RefSeq; WP_011332110.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0444; -.
DR   PRIDE; Q3KJ68; -.
DR   EnsemblBacteria; ABA72188; ABA72188; Pfl01_0444.
DR   KEGG; pfo:Pfl01_0444; -.
DR   eggNOG; ENOG4105CNG; Bacteria.
DR   eggNOG; COG0397; LUCA.
DR   HOGENOM; HOG000008335; -.
DR   OMA; RMHAVNP; -.
DR   BioCyc; PFLU205922:G1G4S-449-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00692; SelO; 1.
DR   InterPro; IPR003846; SelO.
DR   PANTHER; PTHR32057; PTHR32057; 1.
DR   Pfam; PF02696; UPF0061; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ68.
DR   SWISS-2DPAGE; Q3KJ68.
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..487
FT                   /note="Protein adenylyltransferase SelO"
FT                   /id="PRO_0000271847"
FT   NP_BIND         90..93
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   NP_BIND         125..126
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   METAL           253
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   METAL           262
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         113
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         176
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         183
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ   SEQUENCE   487 AA;  55089 MW;  924E64A45219B291 CRC64;
     MKALDELTFD NRFARLGDAF SAHVLPEPID NPRLVVASPA ALALLDLDPA MADTQEFAEL
     FGGHKLWADA EPRAMVYSGH QFGGYTPQLG DGRGLLLGEV YNAAGEHWDL HLKGAGQTPF
     SRMGDGRAVL RSSIREFLAS EALHALNIPS SRAACVIGSD TPVWREKQER AAMVLRLAPS
     HIRFGHFEYF YYTKRPEQQK LLGEHVLAMH YPECLEQPEP YLAMFREIVE RNAELIAKWQ
     AYGFCHGVMN TDNMSILGIT FDFGPFAFLD DFDANFICNH SDDQGRYSFS NQVPVGQWNL
     STLAQALTPL ISVEALRETL GLYLPLFQAH YLDLMRRRLG FTTAEDDDQM LLEQLLQLMQ
     NSGVDYTLFF RRLGEESAEQ AVARLRDDFV DIKGFDAWGE RYVARVARDG ATDQEQRRAR
     MHAVNPLYIL RNYLAQKAID AAEQGDYSEV RRLHAVLSNP FEEQPGMESY AERPPEWGKH
     LEISCSS
//

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