ID A0A942CTC4_UNCAI Unreviewed; 865 AA.
AC A0A942CTC4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 29-MAY-2024, entry version 7.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
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|HAMAP-Rule:MF_00277,
KW ECO:0000313|EMBL:MBS1865939.1}; 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
//