ID   GLNE_SHISS              Reviewed;         946 AA.
AC   Q3YXI9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Glutamate-ammonia-ligase adenylyltransferase;
DE            EC=2.7.7.42;
DE   AltName: Full=[Glutamate--ammonia-ligase] adenylyltransferase;
DE   AltName: Full=Glutamine-synthetase adenylyltransferase;
DE            Short=ATase;
GN   Name=glnE; OrderedLocusNames=SSON_3190;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Adenylation and deadenylation of glutamine synthetase
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + [L-glutamate:ammonia ligase (ADP-
CC       forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase
CC       (ADP-forming)].
CC   -!- SIMILARITY: Belongs to the glnE family.
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DR   EMBL; CP000038; AAZ89773.1; -; Genomic_DNA.
DR   RefSeq; YP_312008.1; -.
DR   GeneID; 3669346; -.
DR   GenomeReviews; CP000038_GR; SSON_3190.
DR   KEGG; ssn:SSON_3190; -.
DR   HOGENOM; Q3YXI9; -.
DR   OMA; Q3YXI9; WERYAMI.
DR   BioCyc; SSON300269:SSO_3190-MON; -.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransfer...; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00802; -; 1.
DR   InterPro; IPR005190; GlnE.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Nucleotide-binding;
KW   Nucleotidyltransferase; Repeat; Transferase.
FT   CHAIN         1    946       Glutamate-ammonia-ligase
FT                                adenylyltransferase.
FT                                /FTId=PRO_1000047017.
FT   REGION       91    302       GlnE 1.
FT   REGION      609    830       GlnE 2.
SQ   SEQUENCE   946 AA;  108317 MW;  FF6C8C9B0BEB1947 CRC64;
     MKPLSSPLQQ YRQTVVERLP EPLAEEPLSA QAKSVLTFSD FVQDSIIAHR EWLTELESQP
     PQADEWQHYA AWLQEALSNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS
     YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW
     PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA
     ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
     GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSCSLL PTLSAIAALH
     LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA
     LTAHMNNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
     LTLISDFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
     YLELLSEFPA ALNHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
     YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
     AWVQMVARYG KPNHLNDREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
     EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSTEA FADYQKNEAW
     TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGRTL QTEVREMREK MRAHLGNKHR
     DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
     TRAYTTLRDE LHHLALQELP GHVSGDCFTA ERDLVRASWQ KWLVEE
//