ID GLNE_XANOM Reviewed; 941 AA. AC Q2NY41; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=XOO4031; OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=342109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.; RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests RT contribution of large numbers of effector genes and insertion RT sequences to its race diversity."; RL Jpn. Agric. Res. Q. 39:275-287(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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008229; BAE70786.1; -; Genomic_DNA. DR RefSeq; YP_453060.1; -. DR GeneID; 3859666; -. DR GenomeReviews; AP008229_GR; XOO4031. DR KEGG; xom:XOO_4031; -. DR HOGENOM; Q2NY41; -. DR OMA; Q2NY41; WERYAMI. DR BioCyc; XORY342109:XOO4031-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 1 941 Glutamate-ammonia-ligase FT adenylyltransferase. FT /FTId=PRO_1000047019. FT REGION 92 301 GlnE 1. FT REGION 599 815 GlnE 2. SQ SEQUENCE 941 AA; 102911 MW; D4421D0377DB2845 CRC64; MSIPTASLSP ALAALIERAV ARVRQSLPAW QVWPGGDFDR QLAQVALASD FALDTLARQP ALLQHLAHPD PPPLPLPQLD PAQPQLWPAQ LRRYRSAEST RLVWRDVLGL DSVEATLAGA TRLAEHCMQC GLQALEQQFA TRHGKVIADD GSVQRLVVFG LGKLGGGELN FSSDVDLVYA YPQGGQSDGA RSLAAEEYFA RLGQQLARLL DEATAEGFSH RVDLRLRPFG TAGRVALSFA GMDQYFQREG RDWERYAWLK ARAVAGAIDA GEAWLETLRP FVYRRYLDFT ALDGLREMKA AITAEVARHD CLDDIKRGPG GIREIEFLAQ SLQLIRGGRE PSLRERRLLP ALRALVTAGQ IDQENGQALT TAYRFLRRLE NRLQMLRDAQ THALPQAPLD RERIALGLGY AEWATLLDAL APQRARVTAE FAELLAPRVR ATAPDTLADY WRALPAGDAA RLAGMGLSDP GGAHQALADF AHSSGVRGLS DSARARLDRV MPALLHAATR ASQPDAAVPR MLGLLQATLR RTSYLSLLDE QPSALARLVD VLSRSALLAE RLAAYPLLLD ELLDTRISGP LPDRAALHAA CADIVHIDDT EAALRELNER RLARSFRIAL ATLDGRQQAV ESTRQLAWLA EAVVQTVLHL ARTEMVAAHG YVSGGSFAII GYGSLGGMEL GFGSDLDLVF LYDHPPEVDA SDGKRPLEAG RWFARLAQKV MALLAAETGA GRLYDIDVRL RPDGGKAALV SSLASYREYQ RERAWTWEHQ ALVRARAVAG DAVLCDAFAQ VRRYTLMRVR DTAQLHEDVR KMRARMRTEL DRSDAGRLDL KQGAGGLVDL EFVLQAGVLG LAAQQPQLLD VCDTPALIDA LVQVHWLPDD SAASLHQAHA TLVDAGLSCT LDRRPRLIAP TPAIQQARGT IFNAARVQRL TFPLGKDEAA L //