ID GLND_NOVAD Reviewed; 912 AA. AC Q2GAJ4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=[Protein-PII] uridylyltransferase; DE Short=PII uridylyl-transferase; DE EC=2.7.7.59; DE AltName: Full=Uridylyl-removing enzyme; DE AltName: Full=UTase; GN Name=glnD; OrderedLocusNames=Saro_0682; OS Novosphingobium aromaticivorans (strain DSM 12444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.; RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Modifies, by uridylylation or deuridylylation the PII CC (glnB) regulatory protein (By similarity). CC -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl- CC [protein-PII]. CC -!- SIMILARITY: Belongs to the glnD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000248; ABD25129.1; -; Genomic_DNA. DR RefSeq; YP_495963.1; -. DR GeneID; 3918107; -. DR GenomeReviews; CP000248_GR; Saro_0682. DR KEGG; nar:Saro_0682; -. DR NMPDR; fig|48935.1.peg.1921; -. DR HOGENOM; Q2GAJ4; -. DR OMA; Q2GAJ4; MQHDLFH. DR BioCyc; NARO279238:SARO_0682-MON; -. DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:HAMAP. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR HAMAP; MF_00277; -; 1. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR010043; GlnD_Uridyltrans. DR InterPro; IPR003607; Met-dep_phosphohydro_HD. DR InterPro; IPR006674; Met-dep_phosphohydro_HD_sub. DR InterPro; IPR002934; Nucleotidyltransferase. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR PANTHER; PTHR13734:SF1; GlnD_Uridyltrans; 1. DR Pfam; PF01842; ACT; 2. 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. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Transferase. FT CHAIN 1 912 [Protein-PII] uridylyltransferase. FT /FTId=PRO_1000078807. SQ SEQUENCE 912 AA; 101972 MW; E81AD196FA1A216A CRC64; MLPRIANQRA IVDRRALADA VSAAFAEQGD RSRPAVVELL RGALDSGRAE LARRLEARPS AGTECAHGQA FLVDQLVRVI HDHVVGKVYR ASNRSTGERI AIIAVGGYGR GEMAPHSDVD IAFVTPIKPT SWCEQVIEAI LYFLWDLGLK VGHSSRSLDE VVRMAKSDLT IRTALLEGRY VWGDRDLFDA ASARFWNEVV NGTEKQFVAE KLQERNERHK RLGDSRYVVE PNVKEGKGGL RDLHTLYWIG KYIHKVRDAS ELVDVGLLTA EEYRAFRRAE NFFWAVRCHL HAITRRAEDR LTFDLQREVA MRMNFADRPG KSAVERFMQY FFLQAKQVGS LTGVFLAQLD GQFARQKRSF FASLRSRRKK VGPFFIEGGK LGVPAEDTFQ QDPVRLVELF AVAASEKVEI HPEAMRLARR DAGLIDAAVR KDQRANALFL DVLTSRNDPE TVLRWMNEAG VFGRFVPDFG RVVAQMQFDM YHHYTVDEHT IRAIGLLASI EKGEAKADHP LASEVVGKVA SRRVLYVATL LHDIAKGRRG DHSVLGAEVA MKLCPRLGLS AAETELVAWL VRWHLLMSAT AFKRDLADYK TIADFVNTVQ SQERLRLLLL LTIVDIRAVG PGVWNSWKRQ LLGDLFVSAE EVLRLGHKQH GRAERIIAKK KAVGAILKER DNLIGTVGRQ LGDAYWIAEP EDIIALNLQQ MDQALGELLS VEAHWYPARG ATLVTVLAAD HPGLFYRIAG GIHLAGGNII DARIHTARNG TAVDNFLVQD PLGRPLNEAS QIERLKNAIA DALANRVKLV PQLAARPLAR PRADAFDVRP IVIFDNKASN RFTVIEVGAR DRPALLNRLA RALFEARLIV HSAHIATYGE RAVDTFYVTD VLGEKVDSEA RMKAVEKRLL EAAEDRKVKD AA //