ID B3E6Z9_TRIL1 Unreviewed; 900 AA. AC B3E6Z9; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 22-FEB-2023, entry version 103. 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 OrderedLocusNames=Glov_2691 {ECO:0000313|EMBL:ACD96404.1}; OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter OS lovleyi). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Trichlorobacter. OX NCBI_TaxID=398767 {ECO:0000313|EMBL:ACD96404.1, ECO:0000313|Proteomes:UP000002420}; RN [1] {ECO:0000313|EMBL:ACD96404.1, ECO:0000313|Proteomes:UP000002420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ RC {ECO:0000313|Proteomes:UP000002420}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., RA Ritalahti K.M., Loeffler F.E., Richardson P.; RT "Complete sequence of chromosome of Geobacter lovleyi SZ."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; CP001089; ACD96404.1; -; Genomic_DNA. DR RefSeq; WP_012470734.1; NC_010814.1. DR AlphaFoldDB; B3E6Z9; -. DR STRING; 398767.Glov_2691; -. DR EnsemblBacteria; ACD96404; ACD96404; Glov_2691. DR KEGG; glo:Glov_2691; -. DR eggNOG; COG2844; Bacteria. DR HOGENOM; CLU_012833_1_0_7; -. DR OMA; WIAKYVY; -. DR OrthoDB; 9758038at2; -. DR Proteomes; UP000002420; Chromosome. 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 Gene3D; 1.20.120.330; Nucleotidyltransferases 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 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 TIGRFAMs; TIGR01693; UTase_glnD; 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|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00277}; Reference proteome {ECO:0000313|Proteomes:UP000002420}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00277}. FT DOMAIN 474..590 FT /note="HD" FT /evidence="ECO:0000259|PROSITE:PS51831" FT DOMAIN 714..799 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT DOMAIN 827..900 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT REGION 1..359 FT /note="Uridylyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277" SQ SEQUENCE 900 AA; 102659 MW; 26B83E5B12DA177A CRC64; MPVHPISAAA IFSAGDQRSF EEQRPEILEA CKQFITSSHE EIRQRHAAGA SGTEVVHQLS AVMDAMVSTL FNGILGLMGA DGKRLTGHLT LAAVGGYGRG ELNPYSDVDI MFLHDGSVPV EAVEAFAQKL LYFLWDLRLD VGYSVRTPAD CVEMAAQDTT IKTALIDCRY LAGHQPLFAT LRKTVYSQIL PKASDKFIKE KIAEMRRRRD KYGATIYLLE PNIKEGEGGL RDLQTALWVA QVKYKFDNPK ELVIKGVLSE AELEVYHSAL DHLWRMRNEL HFHTRRKSDQ MNFDLQVHLA TFLGYKDRGK VLAVEDFMRD YYRHAARVEH FSSTLTSRCV WRDEGAAKIL GYFVRRPVGN GCFVLKGELV IPDESIIDKN PAVLMQIFEL AQKHGVTLNI RVKWLIRRSL HLINDKFRRN REVNQSFLNI LRSEKGMADT LRLMHHLEFL NEYIPEFEHI YCKVQHDLYH IYTVDIHTLF AVEQMEKILS GELKKELPLP CAIARQIGKR ELLILSILFH DIGKGEGGGH ADKGADMIPT IARRMGLSKE DSERLEFLVR QHLVFAHISQ RRDLTDERMI MQFARQMVTS ENLKMLFLLT IADVRAVGSD VWTTWKAMLF NELYEKAFNI LERGDFRLEA GTERVRSVRR KVREMVEYDI PAAVAREELR ALPTRYLLSA PLQTIADHLH LLVQLNDKDL VMQVQHEQES GFSSFTICTF DTHGLFSKIT GVMAANGINI LGAQIFTGKN GKILDILQVN SAQGFLITDA ARWQKVEADM ADVLHGTVQV SDLVHRRQRP TLLPAKSARH FPTRIEIDNE VSDEYTVIDI YAHDKVGLLY LITSTINQLG LYIGVSKIST KVDQVADVFY VRDIFGHKIF AEDKLEEIRT SLSWAIDDWQ //