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-MAY-2013, entry version 77.
DE RecName: Full=Probable glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolysing];
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 (By similarity).
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.
CC -!- SIMILARITY: Contains 1 CN hydrolase domain.
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DR EMBL; AE003849; AAF84763.1; -; Genomic_DNA.
DR PIR; C82617; C82617.
DR RefSeq; NP_299243.1; NC_002488.3.
DR HSSP; P08164; 1IH8.
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; ICEDIWG; -.
DR ProtClustDB; PRK13981; -.
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: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 HAMAP; MF_00193; NadE; 1; fused.
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; Ntlse/CNhydtse; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00920; NITRIL_CHT_1; UNKNOWN_1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding.
FT CHAIN 1 545 Probable glutamine-dependent NAD(+)
FT synthetase.
FT /FTId=PRO_0000306413.
FT DOMAIN 5 267 CN hydrolase.
FT NP_BIND 292 299 ATP (By similarity).
FT REGION 269 545 Ligase.
FT ACT_SITE 294 294 By similarity.
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
//
