GenomeNet

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   10-MAY-2017, entry version 94.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_02090};
DE            EC=6.3.5.1 {ECO:0000255|HAMAP-Rule:MF_02090};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_02090};
GN   Name=nadE {ECO:0000255|HAMAP-Rule:MF_02090};
GN   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: Catalyzes the ATP-dependent amidation of deamido-NAD to
CC       form NAD. Uses L-glutamine as a nitrogen source.
CC       {ECO:0000255|HAMAP-Rule:MF_02090}.
CC   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O =
CC       AMP + diphosphate + NAD(+) + L-glutamate. {ECO:0000255|HAMAP-
CC       Rule:MF_02090}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_02090}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC       synthetase family. {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305}.
DR   EMBL; AE003849; AAF84763.1; -; Genomic_DNA.
DR   PIR; C82617; C82617.
DR   RefSeq; WP_010894420.1; NC_002488.3.
DR   ProteinModelPortal; Q9PC24; -.
DR   SMR; Q9PC24; -.
DR   STRING; 160492.XF1961; -.
DR   EnsemblBacteria; AAF84763; AAF84763; XF_1961.
DR   GeneID; 1127512; -.
DR   KEGG; xfa:XF_1961; -.
DR   PATRIC; 24134135; VBIXylFas578_2090.
DR   eggNOG; ENOG4105C4K; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   eggNOG; COG0388; LUCA.
DR   KO; K01950; -.
DR   OMA; RGVMLPF; -.
DR   OrthoDB; POG091H00G3; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000000812; Chromosome.
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   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   HAMAP; MF_02090; NadE_glutamine_dep; 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   PANTHER; PTHR23090; PTHR23090; 1.
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       Glutamine-dependent NAD(+) synthetase.
FT                                /FTId=PRO_0000306413.
FT   DOMAIN        5    267       CN hydrolase. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   NP_BIND     292    299       ATP. {ECO:0000255|HAMAP-Rule:MF_02090}.
FT   REGION      269    545       Ligase.
FT   ACT_SITE     46     46       Proton acceptor; for glutaminase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   ACT_SITE    113    113       For glutaminase activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_02090}.
FT   ACT_SITE    151    151       Nucleophile; for glutaminase activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_02090}.
FT   BINDING     119    119       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   BINDING     177    177       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   BINDING     183    183       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   BINDING     375    375       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   BINDING     399    399       ATP. {ECO:0000255|HAMAP-Rule:MF_02090}.
FT   BINDING     404    404       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
FT   BINDING     516    516       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_02090}.
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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