ID   GLND_PSEPG              Reviewed;         900 AA.
AC   B0KS97;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
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=PputGB1_1144;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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; CP000926; ABY97052.1; -; Genomic_DNA.
DR   RefSeq; YP_001667388.1; -.
DR   GeneID; 5868903; -.
DR   GenomeReviews; CP000926_GR; PputGB1_1144.
DR   KEGG; ppg:PputGB1_1144; -.
DR   OMA; B0KS97; MQHDLFH.
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    900       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_1000078808.
SQ   SEQUENCE   900 AA;  102573 MW;  7650D665F9A853D7 CRC64;
     MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRLAGEVLD KRFRAGSEIR PLIEARAWLV
     DNILQQAWNQ FDWGDQSGIA LVAVGGYGRG ELHPHSDIDL LILLGAAEHE QYRDAIERFL
     TLLWDIGLEV GQSVRTVDEC AEQARADLTV ITNLMESRTI CGPEALRQRM LEVTSTAHMW
     PSKEFFLAKR AELKARHHKY NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QYGTLNLHAL
     AGEGFLLESE NELLASSQDF LWKVRYALHM LAGRAEDRLL FDHQRSLATL LGYGDDNPKR
     AIEQFMQQYY RVVMSISQLC DLIVQHFEEV ILADEESGST QPLNARFRLH DGYIEAANPN
     VFKRTPFAML EIFVLMAQRP EIKGVRADTV RLLREHRHLI DDTFRTDIRN TSLFIELFKC
     EIGIHRNLRR MNRYGILGRY LPEFGLIVGQ MQHDLFHIYT VDAHTLNLIK HLRKLQYTPV
     SEKFPLASKL MGRLPKPELI YLAGLYHDIG KGRQGDHSEI GAVDAQKFCE RHQLPAWDSR
     LIVWLVQNHL VMSTTAQRKD LSDPQVINDF ALHVGDETRL DYLYVLTVAD INATNPSLWN
     SWRASLLRQL YTETKRALRR GLENPLDREE QIRQTQSSAL DILVREGTDP DDVEQLWSQL
     GDDYFLKHNA ADVAWHTDAI LQQPADGGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV
     TVAAMSQLNL NIHDARIITS SSQFTLDTYI VLDNDGGSIG DNPQRVKQIR DGLTEALRNP
     EDYPTIIQRR VPRQLKHFDF PPQVTILNDA QRPVTILEIT APDRPGLLAR LGRIFLEFDL
     SLQNAKIATL GERVEDVFFI TDADNQPLSD PQLCSRLQEA IVQQLQAGQG SDTSPTRVTF
//