ID   A0A942CTC4_UNCAI        Unreviewed;       865 AA.
AC   A0A942CTC4;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   13-SEP-2023, entry version 4.
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   ECO:0000313|EMBL:MBS1865939.1};
GN   ORFNames=JSS69_08470 {ECO:0000313|EMBL:MBS1865939.1};
OS   Acidobacteriota bacterium.
OC   Bacteria; Acidobacteriota.
OX   NCBI_TaxID=1978231 {ECO:0000313|EMBL:MBS1865939.1, ECO:0000313|Proteomes:UP000724697};
RN   [1] {ECO:0000313|EMBL:MBS1865939.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SZAS LIN-11 {ECO:0000313|EMBL:MBS1865939.1};
RX   PubMed=33819658;
RA   Wang Y., Zhao R., Liu L., Li B., Zhang T.;
RT   "Selective enrichment of comammox from activated sludge using
RT   antibiotics.";
RL   Water Res. 197:0-0(2021).
RN   [2] {ECO:0000313|EMBL:MBS1865939.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SZAS LIN-11 {ECO:0000313|EMBL:MBS1865939.1};
RA   Yin Q.X., Jiang S.L., Li D.X., Yang R., Huang H.L., Tang Q., Wang Y.,
RA   Chen Z.;
RL   Submitted (FEB-2021) 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 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 metabolism.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00277};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC       by glutamine, while glutamine activates uridylyl-removing (UR)
CC       activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBS1865939.1}.
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DR   EMBL; JAFDVY010000038; MBS1865939.1; -; Genomic_DNA.
DR   Proteomes; UP000724697; 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; cd04899; ACT_ACR-UUR-like_2; 1.
DR   CDD; cd04900; ACT_UUR-like_1; 1.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR   HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005105; GlnD_Uridyltrans_N.
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; IPR010043; UTase/UR.
DR   NCBIfam; TIGR01693; UTase_glnD; 1.
DR   PANTHER; PTHR47320; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR47320:SF1; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF03445; DUF294; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF01966; HD; 1.
DR   PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00277};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00277};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_00277};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00277}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00277}.
FT   DOMAIN          448..570
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          685..768
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          797..865
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..332
FT                   /note="Uridylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ   SEQUENCE   865 AA;  97347 MW;  E9192430EBBDD0B9 CRC64;
     MTGPGISLSV LGSRCERERA RIRKEFENGV GARETLHALC DLADEVLQKV FQDALRLHNS
     SAEGLSLLAL GGYGRRMLFP YSDLDILFLF ANDKAEEESR SLISEFSRAM WDLGFRVSSA
     GRTIDECKRI EEDNAEFHLA LLDRRFLDGD KALFEKLDAR ILPPSERQAR PFLFAQLHRL
     TKERLARYGN TIFHLEPNVK EAPGGIRDYQ AAYWLRQILG DRKDLRGSSA AEEQLSADAV
     EFQSSIRCFL HYSNGRNDNA LTYELQAEAA EKSLGIDGGE QRTAAEWMRI YFRHARTLNR
     QLLRYLDQKM TAPLSLKERF FSAARSVTKN EPLASGDYCI RSGQIEVLNQ QALSDRAVMY
     SIFAEAARTG TPLAPQAERS ISYIMTHSEL PVINQAIEWD TLKEILAGDF PGVALRPMHR
     LGLLTEILPE FRAIDSLVVR DFYHRYTVDE HSLRTIEHLQ ELADPPDERG VSFAPLWKTL
     DRRDLLIFAL LLHDTGKGMP AENHVTGSLE ALETAAHRLG LTTEEEAEVH FLIEQHLVMS
     ATVQRRDIFD PSIVSGFAEA VGTLERLQRL TLLTYADIHA VNPEALTPWK AQMLWQLFVA
     TSNHFSRTLD RNRLHASDEK SMLEQVRALM PNTKTADLER FLEGFPRRYL AVHSAAEIAR
     HFAMYQNLGS TPLQTELISE RHGFSLTLLT ADRPALFSTI SGVLAAWGMN IIKADAFANA
     AGVVLDTFHF ADLHRTLELN PTEKERFMTS LHDVLQNRAA LEPLLQSRDA ASRTRPPKVA
     VQTRLSFDDS ASAHSTLLEV VVQDRPGLLY DIGSALTRLG CNIEVALIDT EGQKAIDVFY
     LTSQGKKLTA QKQELLKEVL QGTLG
//