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Database: UniProt
Entry: Q9PC24
LinkDB: Q9PC24
Original site: Q9PC24 
ID   NADE_XYLFA              Reviewed;         545 AA.
AC   Q9PC24;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   01-OCT-2014, entry version 84.
DE   RecName: Full=Probable glutamine-dependent NAD(+) synthetase;
DE            EC=6.3.5.1;
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
GN   Name=nadE; OrderedLocusNames=XF_1961;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A.,
RA   Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R.,
RA   Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A.,
RA   Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P.,
RA   Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C.,
RA   Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A.,
RA   Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L.,
RA   Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y.,
RA   Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B.,
RA   Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S.,
RA   Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A.,
RA   Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B.,
RA   Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M.,
RA   de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E.,
RA   da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr.,
RA   da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A.,
RA   de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H.,
RA   Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L.,
RA   Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
CC   -!- FUNCTION: Can use both glutamine or ammonia as a nitrogen source.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC       AMP + diphosphate + NAD(+) + L-glutamate.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC       synthetase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 CN hydrolase domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00054}.
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DR   EMBL; AE003849; AAF84763.1; -; Genomic_DNA.
DR   PIR; C82617; C82617.
DR   RefSeq; NP_299243.1; NC_002488.3.
DR   RefSeq; WP_010894420.1; NC_002488.3.
DR   ProteinModelPortal; Q9PC24; -.
DR   STRING; 160492.XF1961; -.
DR   EnsemblBacteria; AAF84763; AAF84763; XF_1961.
DR   GeneID; 1127512; -.
DR   KEGG; xfa:XF1961; -.
DR   PATRIC; 24134135; VBIXylFas578_2090.
DR   eggNOG; COG0388; -.
DR   KO; K01950; -.
DR   OMA; EFWGKRS; -.
DR   OrthoDB; EOG6VB6S8; -.
DR   UniPathway; UPA00253; UER00334.
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:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; -; 1.
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; IPR000132; Nitrilase/CN_hydratase_CS.
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.
DR   PROSITE; PS00920; NITRIL_CHT_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    545       Probable glutamine-dependent NAD(+)
FT                                synthetase.
FT                                /FTId=PRO_0000306413.
FT   DOMAIN        5    267       CN hydrolase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00054}.
FT   NP_BIND     292    299       ATP. {ECO:0000250}.
FT   REGION      269    545       Ligase.
FT   ACT_SITE    294    294       {ECO:0000255|PROSITE-ProRule:PRU00054}.
SQ   SEQUENCE   545 AA;  59261 MW;  9EBBB7BA14CA7813 CRC64;
     MSEFLRIAMA QFDFPVGAVA QNAERIIALI EQARDEHGAD VVMFPELALS GYPPEDLLLR
     PGFLAHCQVA IERIAAATHG IVAVVGWPQS AGSVVYNVAS VLCDGQVEQT YRKRELPNYA
     VFDERRYFEV DPNGSRCVFK VKGVPVGVLI CEDLWFSEPL ADTVCGGAEL VLVPNASPYE
     RGKHAQRDAL LAERARETGA AIAYLNVVGG QDALVFDGAS VVVDGHGRVH PAAAAFSDQW
     LVVDYMRSER RFVPLQWVAE SEVSINALVW RAVVRGVQDY CRKNGFSKVW VGLSGGIDSA
     LVLAIAVDAL GADQVTAVRL PSRYTAELSN DLAAEQCHSL GVRLETVAIE PVFEGLLAAL
     GPLFAGMAPD ATEENLQSRS RGVILMALAN KFGGLLLTTG NKSEYAVGYA TIYGDMCGGY
     APLKDIYKSQ VFELAQWRNT VSDVLAIPPG VIHRPPSAEL RAQQTDQDSL PPYEVLDGIL
     SLYVDQEQSR EDIIAAGYAA GVVDYVLNLV KINEWKRHQA APGPKVSQRA FGRERRYPIS
     NAYRG
//
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