SELO_MORMI
ID SELO_MORMI Reviewed; 557 AA.
AC Q9RA11;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 40.
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};
OS Moritella marina (Vibrio marinus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=90736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15381 / BCRC 15891 / CIP 102861 / NCIMB 1144 / MP-1;
RA Tanaka M., Ueno A., Kawasaki K., Yumoto I., Ohgiya S., Hoshino T.,
RA Ishizaki K., Okuyama H., Morita N.;
RT "Isolation of clustered genes that are notably homologous to the
RT eicosapentaenoic acid biosynthesis gene cluster from the docosahexaenoic
RT acid-producing bacterium Vibrio marinus strain MP-1.";
RL Biotechnol. Lett. 21:939-945(1999).
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}.
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DR EMBL; AB025342; BAA89392.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RA11; -.
DR SMR; Q9RA11; -.
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; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..557
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_0000121434"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 101..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 135..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ SEQUENCE 557 AA; 63003 MW; BFCFFF6AAD73C2A7 CRC64;
MRQKTATITR RDKSFTGHYV PVKPTPIKDP EYVAHSKNLF SELGFADSMA ESADFVRMFS
GDMSGVPVPM RQVGWASGYA LSIYGTEYTQ QCPFQTGNGY GDGRAISVLE TLIKGQRWEM
QLKGGGRTPY CRGADGRAVL RSSIREFLAQ DHMHALGVPT SRSLSLYVSK TETVKRPWYS
QGSRSENPDM LISEAVAIST RVAPSFIRVG QLELFARRSR SNEHPKAMEE LEKIVLHLID
REYADVIDTQ LATPEKIVLL AREFRGRLTS MVANWIRVGF CQGNFNSDNC AAGGFTLDYG
PFGFCDVFNP YYQPWTGGGN HFSFMNQPNA AQRNFDMFCS ALRPLLVSHQ QDLLAFDEIQ
SEFLAVMDTK MKAMWATKLG LINLKTESDK ALCNVLIKEL QTLMMQAPVD YTIFFRELSS
IPDDIGPLKK SFYSNLYNDA ADDPDTLALE KYWIEWLEKW QMLLNSTCDA KGISSRASED
IAMQMKLVNP KYVLREWFVM PAYQQATAGD YSLIQELQAV MTQPYAEQSK ELEDKYYRLK
PLEFFEVGGL SHLSCSS
