ID GLND_NITWN Reviewed; 925 AA. AC Q3SWE0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 24. 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=Nwi_0133; OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., RA Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., RA Arp D.J., Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing RT bacterium Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). 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; CP000115; ABA03401.1; -; Genomic_DNA. DR RefSeq; YP_316753.1; -. DR GeneID; 3676202; -. DR GenomeReviews; CP000115_GR; Nwi_0133. DR KEGG; nwi:Nwi_0133; -. DR NMPDR; fig|323098.3.peg.603; -. DR HOGENOM; Q3SWE0; -. DR OMA; Q3SWE0; MQHDLFH. DR BioCyc; NWIN323098:NWI_0133-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; 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 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 1 925 [Protein-PII] uridylyltransferase. FT /FTId=PRO_0000231682. SQ SEQUENCE 925 AA; 104377 MW; 9B4D8076280C0070 CRC64; MVLPTTKDAT AAGAGFDTVR IIGDIDALAE KHAGHEDVFR SAVSRLLKAE LAKVRDAAQA KLLRDRHGRH CAEWLCFVQD EIIRLSFSAA TRHLYHSPIP SDGERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG ILEARFLTGD RALYDELISR FDTEVVQGTA AEFVAAKLAE REERHHRAGQ SRYLVEPNVK DGKGGLRDLH TLFWIAKYVY RVRESHELLR RNVFDVREYR TFRRCADFLW SVRCNLHFAT GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI LCAKLEDQQA KPAPVLSRAM SKPPGAEVRR VPDSDDFIID NNRINLAAPD LFKRDPVNLI RLFRLAQKNN LAFHPDALRM VRRSRRLINA QLREDPESNR LFIEILTSND AETVLRRMNE TGVLGEFIRA FGKIVSMMQF NMYHHYTVDE HLIRCIGILQ DIERGDNDEV ALAGELMRTI NPEHRPVIYI ATLLHDVAKG RPEDHSIAGA RVARRLCPRL GFNAADTELV AWLIEQHLTM SKVAQSRDLS DRKTIENFAA VVQSVERMKL LTILTTADIR GVGPGVWNGW KAQLLRTLYY ETEPVLTGGF SEVNRAQRMA AAEAEFRAAF TEWSGHELNA YIARHYPAYW LKVDLEHKIR HARFLRASEQ SGRKLNINVG FDEARGVTEL TILAADHPWL LSIIAGACAS AGANIVDAQI YTTTDGQALD TIAISREYER DEDEGRRAAR IAEIIEQVLE GRLRLPDVMP SRAAGKRLRP FVVEPKVTIN NQWSDRHTMI EVSGLDRPGL LFQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAR ITAPTRQAAI KRALVHLLAS GNTAE //