GLND_PHOPR
ID GLND_PHOPR Reviewed; 874 AA.
AC Q6LN22;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=PBPRA2970;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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}.
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DR EMBL; CR378672; CAG21304.1; -; Genomic_DNA.
DR RefSeq; WP_011219571.1; NC_006370.1.
DR AlphaFoldDB; Q6LN22; -.
DR SMR; Q6LN22; -.
DR STRING; 298386.PBPRA2970; -.
DR EnsemblBacteria; CAG21304; CAG21304; PBPRA2970.
DR KEGG; ppr:PBPRA2970; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_0_0_6; -.
DR OMA; WIAKYVY; -.
DR OrthoDB; 162558at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; 1.
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; 1.
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..874
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192750"
FT DOMAIN 455..577
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 696..779
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 802..874
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..336
FT /note="Uridylyltransferase"
FT REGION 337..695
FT /note="Uridylyl-removing"
SQ SEQUENCE 874 AA; 100797 MW; BD18CA770614C067 CRC64;
MIDTSTITNP QTLPVEAITQ ENLRNTLEQF AEQQKQQFIQ HRPVTDLVLS RSTFIDKLLI
RLWEHYEVNQ YPDIALVAVG GYGRGELHPL SDVDILILSA QPLSDETGRI VSKFLTFLWD
LRLEVGHSVR TIDDCIEIGN DDLTVATNLT EARILCGSED VFQCLQERIN AGNFWPSEDF
YRAKLEEQKT RHARYHDTTY NLEPDIKSSP GGLRDIHTLS WVARRHFGAT SLLEMSRFGF
LTDAEYRELV ECQDSLWRIR FALHIELRRY DNRLTFSHQP SVAENLGYTG EGNRGVEMMM
KEFYRTLRRV LELNKMLLQL FDQAILDNGK TVETIQLSDD FQIRGHLIEA TKPALFQARP
ETILDMFLHI AQNGDIEGIA APTLRQLRTA RQRLNVFLVD IPEAREKFME LVRQPNTLQK
AFRLMHRHGV LSAYLPQWSQ IVGQMQFDLF HVYTVDEHSV RLIKNLNKFN DPENRERHPI
CCEVYPRIIK KELLTIAAIF HDIAKGRGGD HSELGAIEAR KFCIQHGLSR PETNLIAWLV
QKHLLMSVTA QRRDIYDPEV VAEFAKEVRD EERLDYLICL TVADICATNQ ELWNSWKRTL
LAELYYSTQK ALRRGLENTP DVRDRIRHNQ QLSSAILRGK GFAPREIEVL WKRFKADYFL
RHTHKQLAWH AEALLTHDHD KPLILLSKKA TRGGTEVFVY NKDKAKLFAI VVSELDKKNL
SVHDAQIMNS KDGYTLDTFM VLDPSGKTIP ENRHNTIRRA LVNALTKMKS ERKNKRAPRK
LMHFNVKTQV DFLPTKTGKK TTMELIALDT PGLLARIGAV FAKQKVSLQA AKITTIGERA
EDFFILVNEH GSPLTEEHQQ ALKEALIIKL TPQD
