ID   GLND_NITHX              Reviewed;         931 AA.
AC   Q1QRM1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Nham_0226;
OS   Nitrobacter hamburgensis (strain X14 / DSM 10229).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B.,
RA   Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L.,
RA   Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-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.
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DR   EMBL; CP000319; ABE61126.1; -; Genomic_DNA.
DR   RefSeq; YP_575586.1; -.
DR   GeneID; 4030820; -.
DR   GenomeReviews; CP000319_GR; Nham_0226.
DR   KEGG; nha:Nham_0226; -.
DR   NMPDR; fig|323097.3.peg.666; -.
DR   HOGENOM; Q1QRM1; -.
DR   OMA; Q1QRM1; MQHDLFH.
DR   BioCyc; NHAM323097:NHAM_0226-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    931       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_1000022348.
SQ   SEQUENCE   931 AA;  104795 MW;  4609DB25262D4648 CRC64;
     MDLATTNDAA GAGNDFDTAR ITGDIDALAA KHAGHEDVFR AAVSRLLKAE LAKVRDAAQA
     KLLRDRHGRR CAERLCFIQD EIIRLSFSAA TRHLYHSPIP SDGERMAVVA TGGYGRGLMA
     PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG
     ILETRFLAGD RALYDELVTR FDTEVVQGTA AEFVTAKLAE REERHRRAGQ SRYLVEPNVK
     DGKGGLRDLH TLFWIAKYVY RVHESRELLG CGVFDVREYR TFRRCADFLW SVRCNLHFAT
     GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI LCAKLEDQQA
     KPAPVLGRMM SRRRPGTELR RVPEGDDFII DNNRINLAAP DVFKRDPVNL IRVFRLAQKN
     NLAFHPDALR TVTRSRRLIN AQLRENPEAN RLFMEILTSN DAETVLRRMN ETGVLGHFIR
     AFGKIVSMMQ FNMYHHYTVD EHLLRCIGIL QDIERGGNDE LALASELMRK IHPEHRPVIY
     ITTLLHDIAK GRPEDHSIAG ARVARRLCPR LGFNASDTEL IAWLIEQHLT MSKVAQSRDL
     SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRTLY YETEPVLTGG
     FSEVNRVQRI AEAQAEFRAA FTEWSEPELN AYIARHYPAY WLKVDLAHKI RHARFLRASE
     QGGRKLNINV GFDEARGVTE LTIFAADHPW LLSIIAGACA SAGANIVDAQ IYTTTDGQAL
     DTIAISREYD RDEDEGRRAA RIGEIIEQVI DGRLRLPDVV ARRAAGKTRL RPFVVEPKVI
     VNNQWSDRHT VIEVSGLDRP GLLFQLTAAI SKLNLNIASA HVATFGERAR DVFYVTDLLG
     ARITAPTRQA AIKRALIHLL ANGGAAEQSV G
//