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Database: UniProt/TrEMBL
Entry: E3HR16_ACHXA
LinkDB: E3HR16_ACHXA
Original site: E3HR16_ACHXA 
ID   E3HR16_ACHXA            Unreviewed;       685 AA.
AC   E3HR16;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   29-OCT-2014, entry version 26.
DE   SubName: Full=NAD+ synthetase {ECO:0000313|EMBL:ADP15976.1};
DE            EC=6.3.1.5 {ECO:0000313|EMBL:ADP15976.1};
GN   Name=nadE {ECO:0000313|EMBL:ADP15976.1};
GN   OrderedLocusNames=AXYL_02656 {ECO:0000313|EMBL:ADP15976.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP15976.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP15976.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP15976.1,
RC   ECO:0000313|Proteomes:UP000006876};
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 acids-degrading
RT   bacterium Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|RuleBase:RU003811}.
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DR   EMBL; CP002287; ADP15976.1; -; Genomic_DNA.
DR   RefSeq; YP_003978691.1; NC_014640.1.
DR   ProteinModelPortal; E3HR16; -.
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; IRPSCLQ; -.
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:UniProtKB-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; SSF56317; 1.
DR   TIGRFAMs; TIGR00552; nadE; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00094472};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006876};
KW   Ligase {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00094482};
KW   NAD {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00094452};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00094489};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006876}.
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
//
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