ID A0A1G8LA41_9RHOB Unreviewed; 934 AA.
AC A0A1G8LA41;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04487993_100652 {ECO:0000313|EMBL:SDI52568.1};
OS Salipiger marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI52568.1, ECO:0000313|Proteomes:UP000199093};
RN [1] {ECO:0000313|EMBL:SDI52568.1, ECO:0000313|Proteomes:UP000199093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI52568.1,
RC ECO:0000313|Proteomes:UP000199093};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNEJ01000006; SDI52568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8LA41; -.
DR STRING; 555512.SAMN04487993_100652; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000199093; 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; IPR002934; Polymerase_NTP_transf_dom.
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 Pfam; PF01909; NTP_transf_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:SDI52568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199093};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00277}.
FT DOMAIN 508..630
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 746..826
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 856..934
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..391
FT /note="Uridylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
FT COILED 655..682
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 934 AA; 106301 MW; 9E71228E7DB64753 CRC64;
MTLPPPASPA PVSDLRPEDI LPDDLIAPAA TIFDLPALRA RLFDSLPAEG GEPAIRAATV
RLLNEARHAG RETIAQAFAA QPRNAFPVTH AYTWVTDGLV RLCFEVATEV LHPRPNPTAG
ERLAVLAVGG YGRGEMAPHS DVDLLFLTPH KITAWAESVI ESMLYMLWDL KLKVGHASRT
VKDCLRLGAE DFTIRTAMLE HRYLIGHRPL AEDLDKRLWN DLFKGSERAF VAAKLEERGE
RHRKQGLRYV VEPNVKEGKG GLRDLQSLFW ITKYIHRTDD TEAMVRLGVF RPEEYRTFHK
AEEFLWATRC HMHLATGRAV EQLTFDMQVE VADRMGYVDK GGRRAVEWFM QDYFRHATAV
GDLTRIFLTS LEAEHQKDAP LILRMFKRGP QVKDGYEVVH NRLAIIDPKA FLTDKMNLLR
IFEEALRTGL LIHPDAMRLV KANLTLIDDD MRTDREAQRI FMDLMLKHGN PERALRRMNE
LGVLAAFIPE FEPIVAMMQF NMYHAFTVDE HTIQCIRHLS EIEHGDLTEE LPVASHILRE
GVNRKVIYVA LLLHDIGKGR DEDHAVLGAQ IARRVAPRLG LGKQESATVE WLVRYHLLMS
DMAQKRDIAD PRTVRDFAKA VQTRERLDLL TVLTVCDIRG VGPGVWNNWK AALIRALYRQ
TRRALEDGME ALNRENRGTE AKRALREALA DWDGKDLRTE TQRHYEPYWQ GLHVTAHQVF
ARLLRDIQQD EIKIDIHPDE DRDATRVCFA LQDHPGIFSR LAGALALSGA NVVDARTFTS
KDGYATAAFW IQDADGSPYE SARIPRLRDT IRKTLLGEVK PREAIQSRDK LKKRERAFKV
PTSITFDNEG SDIYTIIEVD TRDRPGLLYD LTRTLAEAHV YIASAVIATY GEQVVDSFYV
KDMFGLKYFS PSKQRTLERK LRDAIAAGAE RARA
//