ID A0A2V2LJ44_9RHOB Unreviewed; 477 AA.
AC A0A2V2LJ44;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Protein adenylyltransferase SelO {ECO:0000256|HAMAP-Rule:MF_00692};
DE EC=2.7.7.108 {ECO:0000256|HAMAP-Rule:MF_00692};
GN Name=selO {ECO:0000256|HAMAP-Rule:MF_00692};
GN ORFNames=DKT77_07035 {ECO:0000313|EMBL:PWR03216.1};
OS Meridianimarinicoccus roseus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meridianimarinicoccus.
OX NCBI_TaxID=2072018 {ECO:0000313|EMBL:PWR03216.1, ECO:0000313|Proteomes:UP000245680};
RN [1] {ECO:0000313|EMBL:PWR03216.1, ECO:0000313|Proteomes:UP000245680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TG-679 {ECO:0000313|EMBL:PWR03216.1,
RC ECO:0000313|Proteomes:UP000245680};
RA Ren Y.;
RT "Rhodobacteraceae gen. nov., sp. nov. isolated from sea water.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Ser, Thr or Tyr residues of target proteins (AMPylation).
CC {ECO:0000256|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; EC=2.7.7.108; Evidence={ECO:0000256|HAMAP-
CC 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=2.7.7.108;
CC Evidence={ECO:0000256|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=2.7.7.108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00692};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00692};
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000256|ARBA:ARBA00009747,
CC ECO:0000256|HAMAP-Rule:MF_00692}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWR03216.1}.
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DR EMBL; QGKU01000029; PWR03216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2LJ44; -.
DR OrthoDB; 9776281at2; -.
DR Proteomes; UP000245680; Unassembled WGS sequence.
DR GO; GO:0070733; F:AMPylase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR PANTHER; PTHR32057:SF14; PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL; 1.
DR Pfam; PF02696; SelO; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00692};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00692};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00692}; Reference proteome {ECO:0000313|Proteomes:UP000245680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00692}.
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 88..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 123..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ SEQUENCE 477 AA; 50388 MW; 91B66780B734378E CRC64;
MTLHIPFDNS YARLPARLFH RQTAEPVSAP TPIVVNGALA AELGLDAAAL AGPEGTAVLA
GNAVPGGADP LAQVYAGHQF GGWNPQLGDG RALLLGEVID TAGRRRDLQL KGSGRTPFSR
MGDGRAWLGP VLREYVVSEA MHAMGIPTTR ALAAVATGEP VLRETGPMPG AVLTRVAASH
IRVGTFQFFA ARGDLEAVRA LTEYAIARHY PQAEDAAGLL EAVIAAQADL VARWLGVGFI
HGVMNTDNCA ISGETIDYGP CAFMDRYEAG KVFSSIDRFG RYAYDRQPDI AVWNLAQFAT
CLLPLIDADQ DRAVDRATEA VHRFPALFAA RRLAVFREKL GLTDIGTPDE DGALIDDLLE
AMEAGGADFT NTFAGLADGI ARAAFADSAP FEALAPRLAA RHAAQGGPDR DAMARANPRL
IPRNHQIEAM IAAAVAGDFA PFRRLNEALA NPFAATPADL AAPPAPHEEV AATFCGT
//
