ID   GLND_COLP3              Reviewed;         878 AA.
AC   Q485H4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=CPS_1549;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ26298.1; -; Genomic_DNA.
DR   RefSeq; YP_268291.1; -.
DR   GeneID; 3520548; -.
DR   GenomeReviews; CP000083_GR; CPS_1549.
DR   KEGG; cps:CPS_1549; -.
DR   NMPDR; fig|167879.3.peg.1810; -.
DR   TIGR; CPS_1549; -.
DR   HOGENOM; Q485H4; -.
DR   OMA; Q485H4; MQHDLFH.
DR   BioCyc; CPSY167879:CPS_1549-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; 1.
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    878       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_0000192729.
SQ   SEQUENCE   878 AA;  101844 MW;  90026DD7C373EF21 CRC64;
     MTSHPVSVHI VPSHFINQLA ISADFLSTRD ICQLSQSFNT WLKDVFIEND INDLLSARAV
     FVDAILKKLW CQHHLDEFQI TLIAVGGYGR GELHPQSDVD ILLLTQEEVD LELEEKISSF
     ITQLWDIKLD IGHSVRSIKE CLKQAVKEVT VATNLMEMRQ VAGNETLTQQ LTPLLSEDVF
     WTSEKFFIAK CKEQEARHQQ YRGAAYTLEP NLKANPGGLR DIQTIAWVAK RHFSADSLEE
     LVEHDYLYPN EFFELLESQD YLWRMRFALH FVAGRSENRL LFDYQADVAK MMGFGDEGKA
     PVERMMKRFF RIIARVTELN TMLLQHFEQA IIKKPELSNI SIINQDFELV DKLINTRNDR
     IFMRPVKMIE MFLIIAQEPG IKGIHSHTMR LMRNARRRLI SGLIDYAECR RMFMAIIRHP
     RGLGLALTLM HRHSILSSYL PLWRNIAGQM QFDLFHAYSV DEHSYRVIKN LHQFSQKEHN
     HKFPLCSKIV QKIRKPEVLY LAGFFHDIGK GRGGDHAKLG AVDALTFCLS HQLSKHDSNM
     VAWLVEHHLL MSVTAQRRDI NDENVIRTFG EIVRDEAHLN YLYCLTVADM RGTNESLWNN
     WKANLLEELY FNTLSAFRHG LEKPVEVRSK IRENQQQALA LLNENNVDEQ SIKALWREFR
     IDYFLRYSPE QIARQCQNIV EHDREKPLVL ISPIPYRGGT EVFIFTKEKN NTFASTVSFL
     VTKKLSIHDA KIITTKTGYT VNTFVVLDSR NKPLRERFYT KEMSQALVDR LQQVNICELP
     EPKLARHMKK FKVPLRVNFI KIHAKNRTMI EIIALDRPGL LSNISQVFLE ARVNIHSAKI
     TTFGEKADDV FTISTEEDDA LTTQEKEALA LRLTQEID
//