ID B3E6Z9_GEOLS Unreviewed; 900 AA. AC B3E6Z9; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 08-JUN-2016, entry version 67. DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277, ECO:0000256|SAAS:SAAS00064648}; 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}; GN Name=glnD {ECO:0000256|HAMAP-Rule:MF_00277}; GN OrderedLocusNames=Glov_2691 {ECO:0000313|EMBL:ACD96404.1}; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. 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., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., RA Fletcher K.E., 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 -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII CC regulatory proteins (GlnB and homologs), in response to the CC nitrogen status of the cell that GlnD senses through the glutamine CC level. Under low glutamine levels, catalyzes the conversion of the CC PII proteins and UTP to PII-UMP and PPi, while under higher CC glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP CC (deuridylylation). Thus, controls uridylylation state and activity CC of the PII proteins, and plays an important role in the regulation CC of nitrogen assimilation and metabolism. {ECO:0000256|HAMAP- CC Rule:MF_00277}. CC -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl- CC [protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277, CC ECO:0000256|SAAS:SAAS00064663}. CC -!- CATALYTIC ACTIVITY: Uridylyl-[protein-PII] + H(2)O = UMP + CC [protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277, CC ECO:0000256|SAAS:SAAS00064667}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00277}; CC -!- ENZYME REGULATION: Uridylyltransferase (UTase) activity is CC inhibited by glutamine, while glutamine activates uridylyl- CC removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277}. CC -!- DOMAIN: Has four distinct domains: an N-terminal CC nucleotidyltransferase (NT) domain responsible for UTase activity, CC a central HD domain that encodes UR activity, and two C-terminal CC ACT domains that seem to have a role in glutamine sensing. CC {ECO:0000256|HAMAP-Rule:MF_00277}. CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP- CC Rule:MF_00277, ECO:0000256|SAAS:SAAS00554649}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000256|HAMAP- CC Rule:MF_00277}. CC -!- SIMILARITY: Contains 2 ACT domains. {ECO:0000256|HAMAP- CC 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 ProteinModelPortal; B3E6Z9; -. DR STRING; 398767.Glov_2691; -. DR EnsemblBacteria; ACD96404; ACD96404; Glov_2691. DR KEGG; glo:Glov_2691; -. DR PATRIC; 21997059; VBIGeoLov31523_2629. DR eggNOG; ENOG4105E1P; Bacteria. DR eggNOG; COG2844; LUCA. DR HOGENOM; HOG000261779; -. DR KO; K00990; -. DR OMA; HTLFWIA; -. DR OrthoDB; EOG6CCH44; -. DR BioCyc; GLOV398767:GH32-2731-MONOMER; -. DR Proteomes; UP000002420; Chromosome. DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR HAMAP; MF_00277; PII_uridylyl_transf; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR InterPro; IPR010043; UTase/UR. 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 TIGRFAMs; TIGR01693; UTase_glnD; 1. DR PROSITE; PS51671; ACT; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002420}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00440795}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00504093}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00440799}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00504094, ECO:0000313|EMBL:ACD96404.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002420}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00504095}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00277, KW ECO:0000256|SAAS:SAAS00504096, ECO:0000313|EMBL:ACD96404.1}. FT DOMAIN 714 799 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 827 900 ACT. {ECO:0000259|PROSITE:PS51671}. FT REGION 1 357 Uridylyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_00277}. FT REGION 358 713 Uridylyl-removing. {ECO:0000256|HAMAP- FT 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 //