ID   GLNE_SALAR              Reviewed;         947 AA.
AC   A9MPW2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 9.
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=SARI_04428;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA   Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX24205.1; -; Genomic_DNA.
DR   RefSeq; YP_001573347.1; -.
DR   GeneID; 5763119; -.
DR   GenomeReviews; CP000880_GR; SARI_04428.
DR   KEGG; ses:SARI_04428; -.
DR   OMA; A9MPW2; WERYAMI.
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    947       Glutamate-ammonia-ligase
FT                                adenylyltransferase.
FT                                /FTId=PRO_1000083701.
FT   REGION       91    302       GlnE 1.
FT   REGION      610    831       GlnE 2.
SQ   SEQUENCE   947 AA;  108157 MW;  6C4402EBC28481D7 CRC64;
     MTPLSSPLRQ YWQTVVERLP EGFTETSLSA QAKSVLTFSD FALDSVIAHP EWLAELESAS
     PQADEWRHYA GWLQEALADV CDDASLMREL RLFRRRIMVR IAWAQALSRV EDETILQQLS
     HLAETLIVGA RDWLYAACCR EWGTPCNPQG VPQPLLILGM GKLGGGELNF SSDIDLIFAW
     PEHGTTQGGR RELDNAQFFT RLGQRLIKAL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA
     ALEDYYQEQG RDWERYAMVK ARIMGDNNDA WSRELRAMLR PFVFRRYIDF SVIQSLRNMK
     GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLNAITALH
     LLPENDVTQL RAAYLFLRRL ENLLQSINDE QTQTLPADDL NRARLAWGMN TDNWPQLVGK
     LTEHMANVRR VFNELIGDDE ADTPQEEELS EPWREVWQDT LQEGDSTPVL AHLADEDRRQ
     LLTLIADFRK ELDKRPIGPR GRQVLDQLMP RLLDDVCSRE DAAVTLSRIT PLLAGIVTRT
     TYLELLSEFP GALKHLIMLC AASPMIASQL ARYPLLLDEL LDPGTLYQPT ATNAYRDELR
     QYLLRVPEED EEQQLEALRQ FKQAQLLRIA AADIAGTLSV MKVSDHLTWL AEAMIDAVVQ
     QAWMQMVARY GQPTHLDERQ GRGFAVVGYG KLGGWELGYS SDLDLIFLHD CPIDVMTNGE
     REIDGRQFYL RLAQRIMHLF STRTSSGILY EVDARLRPSG AAGMLVTSAD AFADYQQHEA
     WTWEHQALVR ARVVYGDPQL TSQFDAVRRT IMTTARDGKT LQTEVREMRE KMRSHLGNKH
     RDRFDIKADE GGITDIEFIA QYLVLRYAHE KPKLTRWSDN VRILELLAQN GIMDEHEAQA
     LTVAYTTLRD ELHHLALQEL PGHVAQTCFS KERALVQASW RKWLVAV
//