(data stored in SCRATCH zone)

SWISSPROT: Q5LWB6_RUEPO

ID   Q5LWB6_RUEPO            Unreviewed;       552 AA.
AC   Q5LWB6;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE            EC=6.3.5.1 {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630};
GN   Name=nadE {ECO:0000256|HAMAP-Rule:MF_02090,
GN   ECO:0000313|EMBL:AAV93744.1};
GN   OrderedLocusNames=SPO0426 {ECO:0000313|EMBL:AAV93744.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93744.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93744.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93744.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to
CC       form NAD. Uses L-glutamine as a nitrogen source.
CC       {ECO:0000256|HAMAP-Rule:MF_02090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP +
CC         diphosphate + H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215;
CC         EC=6.3.5.1; Evidence={ECO:0000256|HAMAP-Rule:MF_02090,
CC         ECO:0000256|PIRNR:PIRNR006630};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family.
CC       {ECO:0000256|RuleBase:RU003811}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD
CC       synthetase family. {ECO:0000256|HAMAP-Rule:MF_02090,
CC       ECO:0000256|PIRNR:PIRNR006630}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02090}.
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DR   EMBL; CP000031; AAV93744.1; -; Genomic_DNA.
DR   RefSeq; WP_011046187.1; NC_003911.12.
DR   STRING; 246200.SPO0426; -.
DR   EnsemblBacteria; AAV93744; AAV93744; SPO0426.
DR   KEGG; sil:SPO0426; -.
DR   eggNOG; ENOG4105C4K; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   eggNOG; COG0388; LUCA.
DR   HOGENOM; HOG000226694; -.
DR   KO; K01916; -.
DR   OMA; CEDIWND; -.
DR   OrthoDB; 1152435at2; -.
DR   BioCyc; RPOM246200:G1G48-433-MONOMER; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR036526; C-N_Hydrolase_sf.
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   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.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWB6.
DR   SWISS-2DPAGE; Q5LWB6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702598};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702604};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630,
KW   ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702606};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02090,
KW   ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811,
KW   ECO:0000256|SAAS:SAAS00702608};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN        5    245       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
FT   NP_BIND     290    297       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE     45     45       Proton acceptor; for glutaminase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   ACT_SITE    113    113       For glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE    149    149       Nucleophile; for glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     175    175       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     181    181       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     373    373       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     397    397       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     402    402       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     521    521       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
SQ   SEQUENCE   552 AA;  60518 MW;  30952267C76DBB99 CRC64;
     MADRFRITLA QLNPTVGDLA GNAAKARMAW EHGREAGADL VALPEMFVTG YNTQDLVLKP
     VFHDAAIAMI EALAEECADG PALAIGGPLV EEGKLYNAYL ILKGGKIVSR SLKTHLPNET
     VFDEVRIFDA GPLGGPYSVG NTRIGSPICE DAWHEDVAET LAETGAEFLL VPNGSPYYRD
     KYDMRINQMV ARVVETGLPL IYLNMVGGQD DQVFDGGTFG LNPGGALAFR MPVFDEAITH
     VDLERGSEGW QIVQGEVAPL PDAWEQDYRV MVESLRDYMR KTGFAKVLLG LSGGVDSALV
     AAIATDALGP ENVRCVMLPS EYTSRSSLDD AEAVAQALGV RYDYVPISES RAAVTNTLAP
     LFAGTEPGLT EENIQSRLRG LLLMALSNKF GEMLLTTGNK SEVAVGYATI YGDMAGGYNP
     IKDLYKTRVF ETCRWRNANH RLWMMGPAGE VIRPSVIDKP PSAELREDQK DSDSLPDYPE
     LDAILDILVD QDGSIADCVA AGFDRDVARR VEHLIYISEY KRYQAAPGAR LTPRAFWLDR
     RYPIVNRWRD PS
//

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