ID A0A2K2FZ30_9SPHN Unreviewed; 916 AA.
AC A0A2K2FZ30;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A8V01_05305 {ECO:0000313|EMBL:PNU04030.1};
OS Novosphingobium guangzhouense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1850347 {ECO:0000313|EMBL:PNU04030.1, ECO:0000313|Proteomes:UP000236327};
RN [1] {ECO:0000313|EMBL:PNU04030.1, ECO:0000313|Proteomes:UP000236327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA925 {ECO:0000313|EMBL:PNU04030.1,
RC ECO:0000313|Proteomes:UP000236327};
RA Sha S.;
RT "Complete genome sequence of Novosphingobium guangzhouense SA925(T).";
RL Submitted (MAY-2016) 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:PNU04030.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LYMM01000040; PNU04030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2FZ30; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000236327; 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; cd00077; HDc; 1.
DR CDD; cd05401; NT_GlnE_GlnD_like; 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; 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; 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; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 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:PNU04030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236327};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00277}.
FT DOMAIN 489..611
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 726..805
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 837..916
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..373
FT /note="Uridylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ SEQUENCE 916 AA; 103948 MW; A995E991B3976A67 CRC64;
MSVIRIPSPR SVIDRRELVQ TIEKLVEAYG AAKGRRYIVE TLRSALAEGR EEIARRLDAK
PSAGHEVAEA QAFLTDQLIR VIHDHVVTNV YPAGNRSKGE RLTIMAVGGY GRGEMAPHSD
VDIAFLTPIK QTPWCEQVIE AMLYFMWDLS LKIGHSSRSL DDMVRMSKSD LTIRTAMLEG
RYVWGDQDLY EEARARFFKD VVSGTERQFV VEKLAEREER HKRMGDSRYV VEPNVKEGKG
SLRDLHTLYW IGKYIHKVRS PAELVDVGLL TAKEYRSFRR AENFFWAVRC HLHTITRRAE
DRLTFDLQRE VAARMNFSDR PGKSAVERFM QMFFLQAKVV GSLTGVFLAQ LDEQFAKRQP
RGLLAGFRAR ERVLKGYKVF GGRLRAPSDD WFAADPVRMI EIFVLAEREG LEIHPETLRL
ISRDAALIKD DVRNDKRAND LFMELLTSRR NPEVALRSFN EAGVFGRFVT EFGRVNAQMQ
FDMYHHYTVD EHTIRAIGLV SRIEKGELKD DHPLAHEVIH KVRSRRALYV SVLLHDIAKG
RKGDHSILGA EIALKLCPRF GLDEEETELV SWLVRHHLLL SATAMKRDLS DGKTIADFVE
VVQSVDRLRQ LTVLTIVDIR AVGPGTWNSW KRQLIATLYG AAEERLRLGH AEFGRPKRVE
AKKAAVEATG PEYAALIEKV GSKFGDAYWI AEPEDVIARN LVQFDASEDE PLSISTEYYP
ARGATLVTVI ASDHPGLFYR IAGGIHLAGG NIIDARIHTT RSGRAVDNFL VQDPLGRPFM
EYAQLRRLEL TIENALANRI KILPQLVAKP DARPRADAFE VRPRVLFDNK ASNRFTVVEI
NARDRPALLN RLAHALFESK LMVHSAHIAT YGERAADTFY VTDLLGEKIT AVPRIKAIER
RLLEAASEPS LEEVEA
//