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Database: UniProt
Entry: A0A225MW55_9BURK
LinkDB: A0A225MW55_9BURK
Original site: A0A225MW55_9BURK 
ID   A0A225MW55_9BURK        Unreviewed;       861 AA.
AC   A0A225MW55;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
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   ORFNames=CEY11_01770 {ECO:0000313|EMBL:OWT65498.1};
OS   Candidimonas nitroreducens.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Candidimonas.
OX   NCBI_TaxID=683354 {ECO:0000313|EMBL:OWT65498.1, ECO:0000313|Proteomes:UP000214603};
RN   [1] {ECO:0000313|Proteomes:UP000214603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-089 {ECO:0000313|Proteomes:UP000214603};
RA   Fan M., Lin Y.;
RT   "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule
RT   of Robinia pseudoacacia in lead-zinc mine.";
RL   Submitted (JUN-2017) 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 metabolism. {ECO:0000256|HAMAP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OWT65498.1}.
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DR   EMBL; NJIH01000002; OWT65498.1; -; Genomic_DNA.
DR   BioCyc; GCF_002209565:CEY11_RS01770-MONOMER; -.
DR   Proteomes; UP000214603; Unassembled WGS sequence.
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; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000214603};
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   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440786, ECO:0000313|EMBL:OWT65498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214603};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:OWT65498.1}.
FT   DOMAIN      440    562       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      679    766       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      790    861       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    321       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
SQ   SEQUENCE   861 AA;  98401 MW;  8BCE601670F496DB CRC64;
     MRASSSSLLA LLRENLQRKR REAIDQFRIH LRPELLLTAL RRATDQAVRE AIKLHPLPAH
     ASLVAVGGYG RGELYPYSDV DVLILLRDPP GQADTRLLEA LVAALWDLGL DLGHSVRTIE
     DCRREAAGDI TVETALMEAR WLAGSKELLQ ALTHAMTEQM DAQTFFQAKR AEMQQRHARH
     QDTPYALEPN CKEAPGGLRD LQVILWLAQA AGLGHTWKEI ARAQLLTAAE YRSLRKADLA
     FKRLRIELHL LCGRREDRVL FDLQPALAAI YGFTATKTRR PSEILMQRYY WAARVVNQLN
     TILMQTFEER LFPQPDAPVH RIDDDFCMVQ NRLELCREDG FERKPTMLLR AFLVMQERPE
     LSGLSAHTLR AMWHARRRID AQFRKNPVNR RLFLQILQQP RGIVHALRRM TMLNILPRYL
     PVFRRIVGQM QHDLFHAYTV DQHILMVIRN LRRFTMPEHA QEYPLASQLM AGVQRHWLLY
     VAALFHDIAK GRGGHHSELG ARDAYRFCIE HGLDEQDTAL VEFLVREHLT MSAYAQKRDL
     SDPQVVREFA AIVGDERRLT TLYLLTVADI RGTSPKVWNS WKGKLLEDLY RQTLLALGGS
     QPDTRTVLSQ RKEAAAAEIR RMGLRDESRE AFWSELDVAY FLRHEASEIA WHTRHLYYRA
     NSPEPVVKAR IAGSSEGLQL MVYTRDAQDL FVTICGYFER RALSVQDARI HTTRHGWALD
     SFVVLPPAHE KDFRSQAALI EHELPELLAG AAPLRHAAAP PRRAGSRRAR VFPIVPNIEL
     QPDENSTSWR LSITASDRPG LLYALAQVFA EHGINLKMAK VMTLGDRVED VFIIAGSALG
     HPRLQLRFER ALLSTLDESG A
//
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