ID E3HR16_ACHXA Unreviewed; 685 AA.
AC E3HR16;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 01-MAY-2013, entry version 19.
DE SubName: Full=NAD+ synthetase;
DE EC=6.3.1.5;
GN Name=nadE; OrderedLocusNames=AXYL_02656;
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8;
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acid-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- SIMILARITY: Belongs to the NAD synthetase family.
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DR EMBL; CP002287; ADP15976.1; -; Genomic_DNA.
DR RefSeq; YP_003978691.1; NC_014640.1.
DR EnsemblBacteria; ADP15976; ADP15976; AXYL_02656.
DR GeneID; 9896988; -.
DR KEGG; axy:AXYL_02656; -.
DR PATRIC; 42558368; VBIAchXyl160325_2662.
DR HOGENOM; HOG000051304; -.
DR KO; K01950; -.
DR OMA; FLALHAW; -.
DR BioCyc; AXYL762376:GJUB-2656-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IEA:EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; Ntlse/CNhydtse; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding.
SQ SEQUENCE 685 AA; 74806 MW; 0BCE1184EE2A9C01 CRC64;
MSNPFFNLYS HGFARVAVGV PECKVADPAF NAAQTIALAQ QAAQGGAVLA AFPELGLSAY
TCDDLFHQKA LLDECEEALA RVVAATAEMD IAVVVGAPLR VAHQLFNCAV VAAGGRVLGV
VPKSYLPNYG EFYEARQFSA GDCAIVSEIS LLGQTVPFGS ELIFQMEKLP LFQFHVEICE
DVWVPIPPSS FAALAGATVL VNLSASNIVV GKSDYRHQLV AQQSARCLSA YMYTSAGRGE
SSTDMAWDGQ ALIYENGELL GESERFLGHS HLLFSDVDLE RLSRERMRQT TFGQSVRRHQ
DEVRKFRSVA VPVNPPLEDA ELPLERRVAR FPYVPADPQR RDARCKEVYS IQVQALVQRL
SASGMSKVVI GISGGLDSTH ALLVCAKAMD ALELPRSNIL AVTMPGFATS SRTLQQARKL
MEVVGCTASE IDIRPSCLQM LKDLGHPYAD GKPVYDITFE NVQAGERTNH LFRIANFNNA
IVIGTGDLSE LALGWCTYGV GDHMSHYSVN ASVPKTLITH LVRWVAESGR LGEEGAQVLL
DVLGTDVSPE LVPGGADDKP VQKSEDSIGP YELQDFNLYY TLRYGFAPTK VAFLALAAWR
DREAGAWPEG GHVARNQYDL AAIKRNLKIF LDRFFRLSQF KRSCVPNAPK VGSGGSLSPR
GDWRAPSDSE SVVWMRDAER IPDEA
//