ID A0A0R0AYK7_9GAMM Unreviewed; 518 AA.
AC A0A0R0AYK7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=ARC20_05560 {ECO:0000313|EMBL:KRG46324.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG46324.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG46324.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG46324.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-2015) 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:KRG46324.1}.
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DR EMBL; LLXU01000056; KRG46324.1; -; Genomic_DNA.
DR RefSeq; WP_057644978.1; NZ_PZOY01000007.1.
DR AlphaFoldDB; A0A0R0AYK7; -.
DR STRING; 676599.ARC20_05560; -.
DR OrthoDB; 9776281at2; -.
DR Proteomes; UP000051802; 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:UP000051802};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00692}.
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 100..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 135..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ SEQUENCE 518 AA; 57352 MW; BE9B6D69AB8B44EE CRC64;
MTARFDNRFI QELPGDAETG PRVREVLGAA WSSVMPTPVR APQLLGYSRE VAAALGLDAG
DVADPDFAQV FAGNALWPGM QPWAANYGGH QFGHWAGQLG DGRAISLGEL VGTDGARHEL
QLKGAGRTPY SRGADGRAVL RSSLREFICS EAMHHLGVPT TRALCLVGSG EAVVRDMFYD
GHPKPEPGAL VCRVAPSFIR FGTFELPASR GDTALLRQLA DFTLSRDFPE LTGHGAAREA
EWFGQVCERT ADMVAHWMRV GFVHGVMNTD NLSILGLTLD YGPYGWLEDY DPDWTPNTTD
ASGRRYRFGT QPQVAYWNLG RLAQALAPLF ADASALQDGL DRFVQRYRRR EREHTAAKLG
LADSGDADLV LMEDLRTLMQ QAEMDMTLAF RGLIELDAEA PTLQPLEAAF YDDAKRDAHS
AALATWLQRY AARLREDPLP AAQRRERMRL ANPRYVPRNW LAQETIDRVA QGDTAALANW
LEVLRHPYDD QPGQEAYARH RPEWARVRAG CSMLSCSS
//
