ID   GLNE_XANCP              Reviewed;         937 AA.
AC   Q8P4V7;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=XCC3599;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE012481; AAM42869.1; -; Genomic_DNA.
DR   RefSeq; NP_638945.1; -.
DR   HSSP; P02342; 1MUL.
DR   GeneID; 1000163; -.
DR   GenomeReviews; AE008922_GR; XCC3599.
DR   KEGG; xcc:XCC3599; -.
DR   HOGENOM; Q8P4V7; -.
DR   OMA; Q8P4V7; WERYAMI.
DR   BioCyc; XCAM190485:XCC3599-MON; -.
DR   BRENDA; 2.7.7.42; 281360.
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    937       Glutamate-ammonia-ligase
FT                                adenylyltransferase.
FT                                /FTId=PRO_0000209286.
FT   REGION       91    300       GlnE 1.
FT   REGION      598    814       GlnE 2.
SQ   SEQUENCE   937 AA;  102203 MW;  3A026930D62F380E CRC64;
     MSQPIPSASP ALAALIERAV ARVRHALPAD APWPEGVEHP LARVALASDF VVDTLARQPA
     LLAHLAQPDP PPLPVPRLDP AQPQEWAAQL RRYRAAASAR LVWRDVLGLD DVDATLAGAT
     TLAETCLQCA LQALEQQFST RHGQVIAEDG SVQRLVVFGL GKLGGGELNF SSDVDLVYAY
     PQAGQSDGAR PLAAEEYFAR LGQQLARLLD ETTADGFSHR VDLRLRPFGS AGRVALSFNG
     MDQYFQREGR DWERYAWLKA RAVAGDIAAG EAWLETLRPF VYRRYLDFTA LDGLRDMKAA
     ITAEVAHHAR LDDIKRGPGG IREIEFLAQS LQLIRGGREA SLRERRLLPA LQALVDLGQI
     DPPTGQALAD AYRFLRRVEN RLQMLRDAQT HALPQGEPER ERIALGLGYA HWQALLEALA
     PHRTRVAAEF AELLAPRVHA TAPDTLADYW RALPEGDAAP LLGIGLHDPN NAHHMLADFA
     QSSGVRALSD GARTRLDRVM PALLHAAIRA TQPDAALRRV LGLLQATLRR TSYLALLDEQ
     PSALARLVDV LSRSALLAER LAAYPLLLDE LLDTRISGPL PDRAALHTAC VDTLQIDDTE
     AALRELNERR LALSFRIALA TLDGRQQPVD STQQLAWLAE AVVQTVLQLA RRELVAAHGQ
     VPGGAFAIIG YGSLGGLELG FGSDLDLVFL YDHPREVEAS DGKRPLEAGR WFARLAQKVM
     TLLGAETGAG RLYDIDVRLR PDGGKGALVS SLASYRDYQR DRAWTWEHQA LVRARAVAGD
     AALCEAFVQV RRETLTRVRD PALLHEDVRK MRARMRSELD RSDAGRLDLK QGAGGLVDLE
     FLLQAGVLGQ AAQHPALLLA CATPALIDAL VQVQWLPAES AAPLHHAHAT LVEAGLSCTL
     DRRPRLVVST PPIRDACQIV AAIADAQQLR FQPGKGA
//