ID G6A153_9PROT Unreviewed; 963 AA.
AC G6A153;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=HIMB100_00020220 {ECO:0000313|EMBL:EHI48438.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI48438.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI48438.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(2011).
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:EHI48438.1}.
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DR EMBL; AFXB01000010; EHI48438.1; -; Genomic_DNA.
DR AlphaFoldDB; G6A153; -.
DR STRING; 909943.HIMB100_00020220; -.
DR PATRIC; fig|909943.3.peg.2084; -.
DR eggNOG; COG2844; Bacteria.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000004261; 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; 3.30.70.260; -; 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; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 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:EHI48438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004261};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00277}.
FT DOMAIN 528..650
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 768..849
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 880..956
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..411
FT /note="Uridylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 108498 MW; BC3A429FFC7FC7A5 CRC64;
MINQEYEGAD QQARRTNVST STLENLQSTS VWQSWLAPLE LVKDKQTAGA FNVFDQQLFA
ETAASVFAGK QAKSEQRAAL LELMKTTLAS GRKTLEDKIV DQRDGAIYVG AHAFLLDSII
SGLVTCARQH VFAVEPRFAV MAVGGYGRGE LAPFSDIDLL FVMPQKQTKS DIEFVEFILY
ILWDLGLSVG HASRTVDENL KAASDDVTIR TSLLEMRPLA GNNDLSDKLL KAFKTWLSGQ
PVLDFVEAKL TERDLRHGRF GGTRYAVEPN VKDGKGGLRD LHTLFWITKY AYRLDHVHAM
LTVGILRSSE ARAFAAAQRF LWTVRCFLHL HHGREDDRLT FDAQMQIAPQ MGFSDRSGLR
GVERFMKRYY LAARQVGNLT RIFCAALATD FDQRPRLNLR KFWVAGFSQR PNIKPFSLEG
ERLHLPDKLR FRDNRDLIIE LFYMAQYHEL DIHPDTLRRL TRAVRALNTT ELQSPKTHER
FLAILTDQRN PERVLRLMNE AGWLGKYLPD FGRIVGMMQF DMYHSYTVDE HTIKAVGNIS
DIEQGVLKTI APVASRLIHE LDSRQALFVA VLFHDIAKGR GGDHSVLGAE VAAQLCPLLG
LNAQTTETVV WLIRHHLLMS KTAFRYDLND PQTISDFAAE VQSPERLKLL LVLTVADILA
VGPEIWNGWK ASLMRDLYSR SEAVLGGAAP SEVSALAAAD AMQATRLALS AWDDERFDAH
AQLFYPSYWT NFSTESHLYH ARLAEQFNAG EKKLLIDFKI DDDKESTILV VMAADHPGLF
SRIVGAVAVA GCSIMNARIN TRHDGTILDQ FRIQDKDRQA VIDPQIQNRI AKIIEQSLAG
DISLFRRLQE RSAQITKRQK AMSVPPRVIV SNNRSNTHTV IEVNGADRPG LLYQITYHLV
QLGLQINSAT VSTYGEKVVD VFYVKDVYGL KIEREASQKK IEQTLMGVFD LQQADSRQNG
THS
//