GLND_SALTY
ID GLND_SALTY Reviewed; 890 AA.
AC P23679;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277};
GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; OrderedLocusNames=STM0214;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
RC STRAIN=LT2;
RX PubMed=2250660; DOI=10.1007/bf00265075;
RA Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L.,
RA Miller C.G.;
RT "Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene.";
RL Mol. Gen. Genet. 223:345-348(1990).
RN [3]
RP IDENTIFICATION OF PROTEIN.
RA Robison K.;
RL Unpublished observations (OCT-1992).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory proteins (GlnB and homologs), in response to the nitrogen
CC status of the cell that GlnD senses through the glutamine level. Under
CC low glutamine levels, catalyzes the conversion of the PII proteins and
CC UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC uridylylation state and activity of the PII proteins, and plays an
CC important role in the regulation of nitrogen assimilation and
CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90602; EC=2.7.7.59;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-
CC tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:57865, ChEBI:CHEBI:90602;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC by glutamine, while glutamine activates uridylyl-removing (UR)
CC activity. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- DOMAIN: Has four distinct domains: an N-terminal nucleotidyltransferase
CC (NT) domain responsible for UTase activity, a central HD domain that
CC encodes UR activity, and two C-terminal ACT domains that seem to have a
CC role in glutamine sensing. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39299.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL19178.1; -; Genomic_DNA.
DR EMBL; X55778; CAA39299.1; ALT_FRAME; Genomic_DNA.
DR PIR; S12028; S12028.
DR RefSeq; NP_459219.1; NC_003197.2.
DR RefSeq; WP_001094519.1; NC_003197.2.
DR AlphaFoldDB; P23679; -.
DR SMR; P23679; -.
DR STRING; 99287.STM0214; -.
DR PaxDb; P23679; -.
DR EnsemblBacteria; AAL19178; AAL19178; STM0214.
DR GeneID; 1251732; -.
DR KEGG; stm:STM0214; -.
DR PATRIC; fig|99287.12.peg.227; -.
DR HOGENOM; CLU_012833_0_0_6; -.
DR OMA; WIAKYVY; -.
DR PhylomeDB; P23679; -.
DR BioCyc; SENT99287:STM0214-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR010043; UTase/UR.
DR PANTHER; PTHR47320; PTHR47320; 1.
DR Pfam; PF01842; ACT; 2.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..890
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192766"
FT DOMAIN 468..590
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 709..784
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 816..890
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..349
FT /note="Uridylyltransferase"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..708
FT /note="Uridylyl-removing"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 101
FT /note="H -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 890 AA; 102264 MW; B4BF92D1DC4280D0 CRC64;
MNTLPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA FDSGICAEQL
IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL HPLSDIDLLI LSRKKLPDEQ
AQKVGELLTL LWDVKLDVGH SVRTLEECLL EGLSDLTVAT NLIETRLLIG DVALFLALQK
HIFSEGFWPS DKFYAAKVEE QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF
GATSLDEMVG FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN
YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV DDEFQLRGTL
IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL RHARRHLSQP LCYIPEARTL
FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE
SFAKEETRQR HPLCVDLWPR LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG
LNSRETQLVA WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL RMDNIDEAAL
HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLRQPLVLLS PQATRGGTEI FIWSPDRPYL
FAAVCAELDR RNLSVHDAQI FTTRDGMAMD TFIVLEPDGS PLAADRHDVI RTGLEQTITQ
RSWQPPQPRR QPAKLRHFTV ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI
SLHGARITTI GERVEDLFII ATADRRALNN VLQLEVQQRL TAALNPNDKG
