ID G8QNL5_AZOOP Unreviewed; 503 AA.
AC G8QNL5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 OrderedLocusNames=Dsui_1465 {ECO:0000313|EMBL:AEV25860.1};
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV25860.1, ECO:0000313|Proteomes:UP000005633};
RN [1] {ECO:0000313|EMBL:AEV25860.1, ECO:0000313|Proteomes:UP000005633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC {ECO:0000313|Proteomes:UP000005633};
RX PubMed=22535943; DOI=10.1128/JB.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
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}.
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DR EMBL; CP003153; AEV25860.1; -; Genomic_DNA.
DR RefSeq; WP_014236561.1; NC_016616.1.
DR AlphaFoldDB; G8QNL5; -.
DR STRING; 640081.Dsui_1465; -.
DR KEGG; dsu:Dsui_1465; -.
DR eggNOG; COG0397; Bacteria.
DR HOGENOM; CLU_010245_4_1_4; -.
DR OrthoDB; 9776281at2; -.
DR Proteomes; UP000005633; Chromosome.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00692}.
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 94..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 129..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00692"
SQ SEQUENCE 503 AA; 54322 MW; 2313324002F9E6F9 CRC64;
MSAPTAPAFT FPFDNSYARD LPGFAVPWQP ATVPAPRLLH FNPGLARELG LPLAEATPDQ
LAALFSGNAL PEGASPIAQA YAGHQFGQFS PQLGDGRALL LGEVIDGQGR RRDIAFKGSG
RTPFSRSGDG KAAVGPMLRE VLTGEAMHAL GIPSTRALAV VATGEPVRRQ RPLPGAVLTR
VADSHLRVGT FQFFAAHAGP AQVRQLADYT IARHYPELVG AENGYLELLR AVAERQAALV
ARWMAVGFIH GVMNTDNMSL AGETIDYGPC AFMEAYDPGA VFSSIDRQGR YAYGRQPEIA
AWNLARFAET LLPLIDADME RAVARATAII EAFPARYQEH WLAALKAKLG LPDGGAEAEA
LGGDWLALLQ AQSVDFTLAW RYLGEAAEGR EERLRTLFAD GAALAAWLQR WRRQCTAADG
EGDNARVAGA ARAAAMARHN PWLIPRNHQV EAALDAAEQG DLAPFHHLLG ALAEPYREQP
RYADLAEPAP REFMRTFQTF CGT
//
