ID   GLND_PSEF5              Reviewed;         900 AA.
AC   Q4KHH8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, 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=PFL_1174;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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; CP000076; AAY90461.1; -; Genomic_DNA.
DR   RefSeq; YP_258305.1; -.
DR   GeneID; 3478991; -.
DR   GenomeReviews; CP000076_GR; PFL_1174.
DR   KEGG; pfl:PFL_1174; -.
DR   NMPDR; fig|220664.3.peg.2617; -.
DR   HOGENOM; Q4KHH8; -.
DR   OMA; Q4KHH8; MQHDLFH.
DR   BioCyc; PFLU220664:PFL_1174-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    900       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_0000192753.
SQ   SEQUENCE   900 AA;  103314 MW;  40F0D6C35069651E CRC64;
     MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRQAREVLD TRFRSGREIR RLIEDRAWFI
     DNILQKAWDQ FSWSEDADIA LVAVGGYGRG ELHPYSDIDL LILLDSADHE IFRDSIERFL
     TLLWDIGLEV GQSVRSVDEC AEQARADLTV ITNLMESRTI AGPEHLRQRM LQVTSTEHMW
     PSKDFFLAKR AEQKARHHKY NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLRAL
     AGEGFLVESE NALLASSQEF LWKVRYALHM LAGRAEDRLL LDHQRSIATL LGFEGEDAKQ
     SIESFMQQYY RVVMSIAQLS DLIIQHFEEV ILAPEDEAPP QPINARFQLH DGYIEAINDN
     VFKRTPFAML EIFVLMAQHP EIKGVRADTI RLLREHRHLI DDDFRHDIRN TSLFIELFKC
     EIGIHRNLRR MNRYGILGRY LPEFGFIVGQ MQHDLFHIYT VDAHTLNLIK HLRKMQYTPI
     SEKFPLASKL MGKLPKPELI YLAGLYHDIG KGRHGDHSEI GAVDAEAFCV RHQLPQWDTR
     LIVWLVQNHL VMSTTAQRKD LSDPQVIHDF AQIVVDQTRL DYLYVLTVAD IYATNPTLWN
     SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQSAAL DILVRNGTDP DEVEQLWSQL
     GDDYFLRHTA GDVAWHSDAI LQQPADGGPL VLIKEITQRE FEGGTQIFIY APDQHDFFAV
     TVAAMDQLNL NIHDARIITS SSQFTLDTYI VLDNDGESIG NNPQRVEQIR KGLTDALRNP
     DDYPTIIQRR VPRQLKHFAF APEVTIHNDA QRPVTVLELS APDRPGLLAR IGKIFLEFDL
     SLQNAKIATL GERVEDVFFI TDAHNQPLSD PQLCSRLQDA IVEQLSVSHE PTIEMTRLSI
//