ID GLNE_VIBVY Reviewed; 950 AA. AC Q7MNY4; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, 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=VV0581; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., RA Liao T.-L., Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., RA Shao C.-P., Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine RT pathogen."; RL Genome Res. 13:2577-2587(2003). 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; BA000037; BAC93345.1; -; Genomic_DNA. DR RefSeq; NP_933374.1; -. DR GeneID; 2623349; -. DR GenomeReviews; BA000037_GR; VV0581. DR KEGG; vvy:VV0581; -. DR NMPDR; fig|196600.1.peg.649; -. DR HOGENOM; Q7MNY4; -. DR OMA; Q7MNY4; WERYAMI. DR BioCyc; VVUL196600:VV0581-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 1 950 Glutamate-ammonia-ligase FT adenylyltransferase. FT /FTId=PRO_0000209284. FT REGION 94 305 GlnE 1. FT REGION 611 832 GlnE 2. SQ SEQUENCE 950 AA; 108919 MW; 4E2E3D363CBF6C0C CRC64; MSLPSPLLPV AELAMQNAQQ SGYLEHWPQA LITQFQFISG LSKFVVETVQ RDAQLAEGLP EMLAQESRQE AYRTRLAEQL QACHDEVAGH RVLRQFRNRE MVYIAWKDFT QAWSLEASLS HLSELAEAMI FETYQWQYQL CCQEWGTPTN AQGEAQPMLI IGMGKLGGGE LNFSSDIDLI FTYPENGETQ GARRSIANAQ FFTRLGQRLI KALDQQTFDG FCYRVDMRLR PFGESGPLVM SYAALEDYYQ EQGRDWERYA MIKARVMGRE MYPEYQELRQ MLRPFVFRRY IDFSAIQSLR RMKSMISSEV RRRGLSNNIK LGAGGIREIE FIAQVFQLIR GGREPALRQR GLLVTLEAIK QLQLLEEAQV CHLVEAYKYL RRLENLLQAM ADKQTQTLPD NELEQLALAV AMGYSQWQAL QNDVQQHMAK VHAVFVTLIG DEEDEVSPVE RHFNELWDMA HNPEVIEQIL QNDLACQNAA TMSEQIIQFK ADLAKKTLGP RGREVLNRLM PKLFSAIFAD ADAQFGLPRV LHLLHNIATR TTYLELLDEH PAALTQLVRL CTASPMISEQ LARYPILLDE LIDPQQLYNP IALDAYRTEL RDFLARIPED DVEQQMDALR QFKQICSLRI AAADIAGVLP VMKVSDHLTY LAEAIVEAVV HQAWQQVAEK YGEPTHLKDR EGKGFAVVGY GKVGGWELGY NSDLDVVFLH DCPVNVYTDG KKEIDGRQFY LRLAQRIIHI FSTRTASGIL YEVDTRLRPS GASGLLVCPV DAFEEYQHND AWTWEHQALV RARMIYGDEH LASEFHRVRH QVLAKPREQA KLQKEVADMR AKMRDHLGGK KSDRFMLKQD QGGITDIEFL AQYLVLNYSA EKPKLTRWCD NVRIFETLIA QGVMEEAQAM LLTQAYTTMR DEIHRRNLLN LDADVALDKF VALRQGVSKA WQEWLESSTI //