Y4LH_SINFN
ID Y4LH_SINFN Reviewed; 192 AA.
AC P55548;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable protein adenylyltransferase y4lH;
DE EC=2.7.7.n1;
GN OrderedLocusNames=NGR_a02670; ORFNames=y4lH;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: Probable adenylyltransferase that mediates the addition of
CC adenosine 5'-monophosphate (AMP) to specific residues of target
CC proteins. {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; U00090; AAB91760.1; -; Genomic_DNA.
DR RefSeq; NP_443958.1; NC_000914.2.
DR RefSeq; WP_010875292.1; NC_000914.2.
DR AlphaFoldDB; P55548; -.
DR SMR; P55548; -.
DR STRING; 394.NGR_a02670; -.
DR EnsemblBacteria; AAB91760; AAB91760; NGR_a02670.
DR KEGG; rhi:NGR_a02670; -.
DR PATRIC; fig|394.7.peg.282; -.
DR eggNOG; COG2184; Bacteria.
DR HOGENOM; CLU_080158_0_2_5; -.
DR OMA; FCHFEYI; -.
DR OrthoDB; 1232677at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF02661; Fic; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..192
FT /note="Probable protein adenylyltransferase y4lH"
FT /id="PRO_0000200902"
FT DOMAIN 52..190
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 82..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 192 AA; 22438 MW; CA883199329E0474 CRC64;
MVRYNAVEDP LCYPGTHVLR NRANIPDQNE LDEFEQLMFD SRAREALPDG DLDFAHYRAL
HRHFFQDVYE WAGQTRIIRT GKGENWFCYP EYIEREANRL FAELAARDHL ARTESKEAFA
KGASWFLAEI NAIHPFREGN GRTQLVFLTM LTRYAGYELD ESKLEPKRFL DAMIRSFSGD
LAPLAAEIRR MI