ID GLND_BURTA Reviewed; 858 AA. AC Q2SX00; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 28. 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=BTH_I2025; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) 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; CP000086; ABC39424.1; -; Genomic_DNA. DR RefSeq; YP_442549.1; -. DR GeneID; 3848603; -. DR GenomeReviews; CP000086_GR; BTH_I2025. DR KEGG; bte:BTH_I2025; -. DR TIGR; BTH_I2025; -. DR HOGENOM; Q2SX00; -. DR OMA; Q2SX00; MQHDLFH. DR BioCyc; BTHA271848:BTH_I2025-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 1 858 [Protein-PII] uridylyltransferase. FT /FTId=PRO_1000022336. SQ SEQUENCE 858 AA; 96880 MW; 80780D220D54F576 CRC64; MSASVAAPPP ALSRKAEFKA AKAELLARFQ TATNVTPLMH ALSRATDDAL RRLWHECGLP ATLALVAVGG FGRGELSPHS DVDILVLLPD AHARELDERI ERFIGMAWDL GLEIGSSVRT VDQCIEEASQ DVTVQTSLLE ARRIVGSTAL FERFMLRYRE ALDARAFFQA KVLEMRQRHA KFQDTPYSLE PNVKESPGGL RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE GFLKTLRARL HVIAGRRQDI LVFDLQTQAA ESFGYRPTPA KRASEQLMRR YYWAAKAVTQ LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA ILEAFLLYEA TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRHTFMQIL QQPEGITHAF RLMNQTSVLG RYLLNFRRIV GQMQHDLYHV YTVDQHILMV LRNIRRFAVA EHAHEYPFCS QLIVNFERPW VLYVAALFHD IAKGRGGDHS ALGMTDARRF CREHGIEGGD AALVVWLVQH HLTMSQVAQK QDTSDPEVIK RFADLVGNER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA DIAWQTRVLY RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY FDRNGLSVLD ARVNTTRHGY ALDNFIVTQT ERDVQYRDIA NLVEQQLAAR LAESAPLPEP SKGRLSRLSR TFPITPRVDL RADERGQYYI LSVSANDRPG LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS DNRLQIQVET ELLRAIAV //