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Database: UniProt
Entry: G6A153_9PROT
LinkDB: G6A153_9PROT
Original site: G6A153_9PROT 
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
//
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