ID   GLND_IDILO              Reviewed;         879 AA.
AC   Q5QXT0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=IL0847;
OS   Idiomarina loihiensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=135577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-TR / ATCC BAA-735 / DSM 15497;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV81687.1; -; Genomic_DNA.
DR   RefSeq; YP_155236.1; -.
DR   GeneID; 3173614; -.
DR   GenomeReviews; AE017340_GR; IL0847.
DR   KEGG; ilo:IL0847; -.
DR   NMPDR; fig|283942.3.peg.853; -.
DR   HOGENOM; Q5QXT0; -.
DR   OMA; Q5QXT0; MQHDLFH.
DR   BioCyc; ILOI283942:IL0847-MON; -.
DR   BRENDA; 2.7.7.59; 280818.
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    879       [Protein-PII] uridylyltransferase.
FT                                /FTId=PRO_0000192738.
SQ   SEQUENCE   879 AA;  101332 MW;  7DFEC2D5EA90098B CRC64;
     MANVQEDKDF HGRWPDRTLQ PCLKDYKALL ESYQNWSAAR FVTADIDELV HHRATFFDQL
     ISQLWQQFQL EDEPASILAV GGYGRETLHP GSDIDLLILV GPENAEAEAK LSEKLGQFVT
     FLWDLHLDIG HSVRTIEDCF AQSENDITIA TNLIESRYLS GAESLYNEFH QQLLNDFPWS
     SRDFYQAKLD EQKQRHQQYH STSYNLEPNI KSSPGGLRDI QTVGWIAKRH FRTHSDENLV
     EYGYMTADEF VELRDCMNWL WRIRFALHLE AGKREDRLLF DFQPGVAVRL GYGNDGKASV
     ETMMKDYFKV VLRVSELNQM LLQFFHQAIL GTQDLQHAEH ISDDFAVANK LLTARHDNVF
     DNHCNIIRAF VCIAEHPQIQ GIHSNTIRLL RNARAQLSEP LSHDPECRDL FNQLIQHPRG
     CGLSFALMHH HSVLASYLSQ WQQIVGQMQF DLFHAYTVDE HTFRLVRNLY RFSDEDYQDQ
     FPLCEKLVAQ MDRRYCLYLA GIFHDIAKGR GGDHSELGEM DARNFCHQHG YSEEDAELVA
     WLVRHHLTMS VTAQKRDIHD PEVIQDFANQ VSTPERLDYL YCLTVADIRA TNQSLWNNWK
     ATLLEELYNA TSYLLQQDSN KPTLDIRQKI NENKASAMAL LLSAGFEKAE ILALWGRFTA
     DYFFRHTAEQ ISWHSQHILN LPSEQLPLIL IGDENNYGTT ELFIYHHEEG HLFASVAGVL
     DSQQLNILDA QILATRDGFV MDTFVVLQRD GKPLTEPHRI EEVKQQLLDV LHKRIPVPST
     KRPLSRRMKN FSVATEVTFI PSKHHGRTTF ELVTLDRPGL IAKLAAILQQ QNVILLAAKI
     TTIGEQAEDL FIVTTEQQTA LSDKQKKTLK AKIIKDLEF
//