(data stored in SCRATCH zone)

SWISSPROT: Q13EY3_RHOPS

ID   Q13EY3_RHOPS            Unreviewed;       933 AA.
AC   Q13EY3;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE            Short=UTase/UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=PII uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UTase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=2.7.7.59 {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_00277};
GN   Name=glnD {ECO:0000256|HAMAP-Rule:MF_00277};
GN   OrderedLocusNames=RPD_0116 {ECO:0000313|EMBL:ABE37356.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37356.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37356.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37356.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the
CC       nitrogen status of the cell that GlnD senses through the glutamine
CC       level. Under low glutamine levels, catalyzes the conversion of the
CC       PII proteins and UTP to PII-UMP and PPi, while under higher
CC       glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP
CC       (deuridylylation). Thus, controls uridylylation state and activity
CC       of the PII proteins, and plays an important role in the regulation
CC       of nitrogen fixation and metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-
CC         L-tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:46858, ChEBI:CHEBI:90602;
CC         EC=2.7.7.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-
CC         L-tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:90602; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174764};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00277, ECO:0000256|SAAS:SAAS00609838};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is
CC       inhibited by glutamine, while glutamine activates uridylyl-
CC       removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277,
CC       ECO:0000256|SAAS:SAAS01174765}.
CC   -!- DOMAIN: Has four distinct domains: an N-terminal
CC       nucleotidyltransferase (NT) domain responsible for UTase activity,
CC       a central HD domain that encodes UR activity, and two C-terminal
CC       ACT domains that seem to have a role in glutamine sensing.
CC       {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277, ECO:0000256|SAAS:SAAS01174767}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
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DR   EMBL; CP000283; ABE37356.1; -; Genomic_DNA.
DR   RefSeq; WP_011500549.1; NC_007958.1.
DR   STRING; 316057.RPD_0116; -.
DR   EnsemblBacteria; ABE37356; ABE37356; RPD_0116.
DR   KEGG; rpd:RPD_0116; -.
DR   eggNOG; ENOG4105E1P; Bacteria.
DR   eggNOG; COG2844; LUCA.
DR   HOGENOM; HOG000261779; -.
DR   KO; K00990; -.
DR   OMA; HTLFWIA; -.
DR   OrthoDB; 162558at2; -.
DR   BioCyc; RPAL316057:RPD_RS00585-MONOMER; -.
DR   Proteomes; UP000001818; 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   HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
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   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EY3.
DR   SWISS-2DPAGE; Q13EY3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS01174769};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00204441};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00677267};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00277};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440786, ECO:0000313|EMBL:ABE37356.1};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:ABE37356.1}.
FT   DOMAIN      500    623       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      741    823       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      853    933       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    384       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
FT   COILED       40     67       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   933 AA;  105371 MW;  4FF353DD6CB3918B CRC64;
     MDKVATPPHR PAGDERFDTQ RITAEIAVLA AQHGGNDQAF RNALAQLMKA ELAKARAEAE
     AQLLRDRHGR RCAERLCFVK DEIIRLLFMA ATKYLYNSPT PSSSERMSVV ATGGYGRGLM
     APESDIDLLF ILPYKQTAWG EQVAEVVLYS LWDIGLKVGH ATRSVDECIR QARADMTIRT
     AILETRFLTG DKALYAELVE RFDKEVVEGT AAEFVTAKLA EREERHRRSG QSRYLVEPNV
     KDGKGGLRDL HTLFWIAKYV YRVRETSELL ERGVFDAIEF RTFRRCEDFL WSVRCNLHFL
     TRRAEERLSF DLQREIGVRL GYTSHPGMQD VERFMKHYFL IAKEVGNLTA ILCAKLEDQQ
     AKPAPALSRM MARLRPGATR RRVPESDDFV IDNNRINLAA PDVFKHDPVN LIRIFRLAQK
     NSLAFHPDAM RTVTRSLALI NAQLRDDPEA NRLFIEILTS DNSEPVLRRM NETGVLGRFI
     RAFGRIVSMM QFNMYHSYTV DEHLLRCVGN LQEIERGGND EFMLSSDLTR RIRPDHRAVL
     YVAVLLHDIA KGQPEDHSTA GAKVARRLCP RFGFNAADTE LIAWLIEKHL VMSTVAQSRD
     LSDRKTIENF AAVVESVEQM KLLTILTTAD IRGVGPGVWN GWKAQLLRTL YYETEPVLTG
     GFSEVNRAER IRAAQAEFRA AFTEWPEAEL DAYVARHYPA YWLKVELARK LRHARFLRAS
     EQAGNKLAVN VGFDEARGVT ELTILAVDHP WLLSIIAGAC ASAGANIVDA QIYTTTDGRA
     LDTISIRREY DRDEDEGRRA TRIGEIIEEV LEGKLRLPEA VARRATSSKT KLRAFVVEPE
     ISINNNWSDR YTVIEVSGLD RPGLLYQLTT AISKLNLNIA SAHVATFGER ARDVFYVTDL
     LGAQITAPTR QAAIKRALVH LLANGDAEQK PAA
//

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