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Bifunctional uridylyltransferase/uridylyl-removing enzyme (UTase/UR) (Bifunctional [protein-PII] modification enzyme) (Bifunctional nitrogen sensor protein) [Includes: [Protein-PII]-UMP uridylyl-removing enzyme (UR) (EC 3.1.4.-); [Protein-PII] uridylyltransferase (PII uridylyltransferase) (UTase) (EC 2.7.7.59)]

 U2WAR3_9PROT            Unreviewed;       933 AA.
U2WAR3;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
12-SEP-2018, entry version 40.
RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
Short=UTase/UR {ECO:0000256|HAMAP-Rule:MF_00277};
AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000256|HAMAP-Rule:MF_00277};
Includes:
RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
Short=UR {ECO:0000256|HAMAP-Rule:MF_00277};
EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_00277};
Includes:
RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
Short=PII uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
Short=UTase {ECO:0000256|HAMAP-Rule:MF_00277};
EC=2.7.7.59 {ECO:0000256|HAMAP-Rule:MF_00277};
Name=rpmI {ECO:0000313|EMBL:ERL46674.1};
Synonyms=glnD {ECO:0000256|HAMAP-Rule:MF_00277};
ORFNames=RS24_01682 {ECO:0000313|EMBL:ERL46674.1};
Candidatus Micropelagos thuwalensis.
Bacteria; Proteobacteria; Alphaproteobacteria; PS1 clade;
Candidatus Micropelagos.
NCBI_TaxID=1397666 {ECO:0000313|EMBL:ERL46674.1, ECO:0000313|Proteomes:UP000016762};
[1] {ECO:0000313|EMBL:ERL46674.1, ECO:0000313|Proteomes:UP000016762}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RS24 {ECO:0000313|EMBL:ERL46674.1,
ECO:0000313|Proteomes:UP000016762};
PubMed=24785133; DOI=10.1111/1574-6941.12348;
Jimenez-Infante F., Ngugi D.K., Alam I., Rashid M., Baalawi W.,
Kamau A.A., Bajic V.B., Stingl U.;
"Genomic differentiation among two strains of the PS1 clade isolated
from geographically separated marine habitats.";
FEMS Microbiol. Ecol. 89:181-197(2014).
-!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
regulatory proteins (GlnB and homologs), in response to the
nitrogen status of the cell that GlnD senses through the glutamine
level. Under low glutamine levels, catalyzes the conversion of the
PII proteins and UTP to PII-UMP and PPi, while under higher
glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP
(deuridylylation). Thus, controls uridylylation state and activity
of the PII proteins, and plays an important role in the regulation
of nitrogen metabolism. {ECO:0000256|HAMAP-Rule:MF_00277}.
-!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl-
[protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00911957}.
-!- CATALYTIC ACTIVITY: Uridylyl-[protein-PII] + H(2)O = UMP +
[protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00911954}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00609838};
-!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is
inhibited by glutamine, while glutamine activates uridylyl-
removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277}.
-!- DOMAIN: Has four distinct domains: an N-terminal
nucleotidyltransferase (NT) domain responsible for UTase activity,
a central HD domain that encodes UR activity, and two C-terminal
ACT domains that seem to have a role in glutamine sensing.
{ECO:0000256|HAMAP-Rule:MF_00277}.
-!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
Rule:MF_00277, ECO:0000256|SAAS:SAAS00911952}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ERL46674.1}.
-----------------------------------------------------------------------
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EMBL; AWXE01000004; ERL46674.1; -; Genomic_DNA.
RefSeq; WP_021777652.1; NZ_AWXE01000004.1.
EnsemblBacteria; ERL46674; ERL46674; RS24_01682.
PATRIC; fig|1397666.3.peg.1570; -.
Proteomes; UP000016762; Unassembled WGS sequence.
GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-UniRule.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
CDD; cd00077; HDc; 1.
HAMAP; MF_00277; PII_uridylyl_transf; 1.
InterPro; IPR002912; ACT_dom.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
InterPro; IPR010043; UTase/UR.
PANTHER; PTHR13734:SF45; PTHR13734:SF45; 1.
Pfam; PF08335; GlnD_UR_UTase; 1.
Pfam; PF01966; HD; 1.
PIRSF; PIRSF006288; PII_uridyltransf; 1.
SMART; SM00471; HDc; 1.
TIGRFAMs; TIGR01693; UTase_glnD; 1.
PROSITE; PS51671; ACT; 2.
PROSITE; PS51831; HD; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000016762};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00911959};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00504093};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00677267};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00504094};
Repeat {ECO:0000256|SAAS:SAAS00471030};
Ribonucleoprotein {ECO:0000313|EMBL:ERL46674.1};
Ribosomal protein {ECO:0000313|EMBL:ERL46674.1};
Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
ECO:0000256|SAAS:SAAS00504094}.
DOMAIN 493 615 HD. {ECO:0000259|PROSITE:PS51831}.
DOMAIN 735 817 ACT. {ECO:0000259|PROSITE:PS51671}.
DOMAIN 845 925 ACT. {ECO:0000259|PROSITE:PS51671}.
REGION 1 376 Uridylyltransferase. {ECO:0000256|HAMAP-
Rule:MF_00277}.
SEQUENCE 933 AA; 105653 MW; D25864CEE78AE1DD CRC64;
MKTKQSQKLK KPHTAGKIRK EFDKIARDHM NVSDDALNQS KARALEMLKK TLAKGHARAH
KNLLNRIYRG GKCAEVISTL MDDIIVELAR FANNLLKGED GQPISCAIVA VGGYGRQRLA
PGSDIDLLFI TPPNADKASL EVVEFILYML WDMGLKVGHA TRDVEDCIFQ AKEDMTTRTA
MLESRFLTGD EVLFTKFRKK FAGKILSGSA RNFVKAKLDE RDLRHKRSGE SRYLVEPNVK
EGKGGLRDLN TLFWIAKYCY AVDTVDELVS CGFLSREELN LFKRCDNFLW AVRCHLHFLT
GRAEERLGFD NQSAMAEAMG FRSTSGLSKV ERFMRQYFLI AKDVGDLTRI FCARLEAEQT
KPGRMARLPA LFQRQKQVHG FTISGQRLTM VRSDVFRRNP VNLIRMFKIA NDYKLLIDPN
TLREVTRSRH LIDKNLRENP EANKLFLEIL TSRNHPERIL RRMNEAGVLG KLLPDFGRIV
AMMQFNMYHH YTADEHLLRA IGILSELERG ELEDDSPLAH RLMSQNINRK VIYLAVLLHD
IAKGRPEDHS LAGARIARRL GPRLGLTKNE TELVAWLVEF HLVMSDTAQR RDLTDPQTIE
DFVSSVQTLE RLRHLLVLTV VDIRAVGPGV WNGWKGQLLR ELYFEAEALL VGSASHANRP
LRVANAQKEF LDVLKKNMPD WAEAQCKKYI ARHHDAYWLS YDIDTKIKHA TLLSSVEDSA
FQIEVTEDKK QEILELNFTC PDHPGLFSRL SGACAVAGLT IVDAKLAITK DGMALDVLRL
QEPERENFPD KARVKRLIAT IKSVLQGDIL PPDRLADVPF SRRVNAFNVV NNVTIDNELS
SHSTVIEVSG LDRPGLLYAL AKTLFNLNVT IVSARAVTFG ERAVDVFYVQ DLTGEKIKRK
SKLTAIMDGL EMVLANQSNP KRAKPAKQGR KAA


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