GLND_RHOPA
ID GLND_RHOPA Reviewed; 929 AA.
AC P62223;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=RPA0591;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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 fixation and metabolism.
CC {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=CAE26035.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX572594; CAE26035.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P62223; -.
DR SMR; P62223; -.
DR IntAct; P62223; 1.
DR MINT; P62223; -.
DR STRING; 258594.RPA0591; -.
DR PRIDE; P62223; -.
DR EnsemblBacteria; CAE26035; CAE26035; RPA0591.
DR KEGG; rpa:RPA0591; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_1_0_5; -.
DR PhylomeDB; P62223; -.
DR Proteomes; UP000001426; 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:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.460.10; -; 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; 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; Nitrogen fixation;
KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..929
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192762"
FT DOMAIN 495..618
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 736..818
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 849..929
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..379
FT /note="Uridylyltransferase"
FT REGION 380..735
FT /note="Uridylyl-removing"
SQ SEQUENCE 929 AA; 104542 MW; BC13BFA4845F8785 CRC64;
MSPSRPAADE RFDSARVAAE IATLAEKHTG NDAAFRTALA MLMKAELAKA RTEAEAQLLR
DRHGRRCAER LCYVQDAIIR LLFNAATEYL YNTPTPSSSE RMTVVATGGY GRGLMAPESD
IDLLFILPYK QTAWGEQVAE VILYCLWDIG LKVGHATRSV DECIRQARAD MTIRTAILET
RFLAGDEALY AELVERFDKE VVEGTAAEFV AAKLAEREER HRRSGQSRYL VEPNVKDGKG
GLRDLHTLFW IAKYVYRVRE ASELSERGVF DPAEFRTFRR CEDFLWSVRC NIHFVTKRAE
DRLSFDLQRE IGVRLGYTSH PGMQDVERFM KHYFLIAKEV GNLTAILCAK LEDQQAKAAP
ALTRMMARLR PAAKRRRVPE SDDFVIDNNR INLAVPDVFK HDPVNLIRIF RLAQKNNLAF
HPDAMRSVTR SLSLITPQLR DNPEANRLFV EILTSDNAEP VLRRMNETGV LGRFIRAFGR
IVSMMQFNMY HSYTVDEHLI RCVGNLQEIE RGGNDEFALS SELIRKIRPD HRAVLYAAVL
LHDIAKGQPE DHSTAGAKVA RRLCPRFGFS TADTELVAWL IEKHLVMSTV AQSRDLSDRK
TIENFAAVVE TVEQMKMLTI LTTADIRGVG PGVWNGWKAQ LIRTLYYETE PVLTGGFSEV
NRAERIRAAQ AEFRAAFTEW PEADLNAYVA RHYPAYWLKV DLQRKIRHAR FLRASEQAGH
KLAINVGFDE ARAVTELTIL AVDHPWLLSV IAGACASAGA NIVDAQIYTT TDGRALDTIS
ISREYDRDED EGRRATRIGE TIEEVLEGKL RLPEAVARRA SSGSKAKLRA FVVEPEVEIN
NNWSDRYTVI EVSGLDRPGL LYQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAQ
ITAPTRQAAI KRALVHLLAN GDAAEKPAA
