(data stored in SCRATCH zone)

SWISSPROT: A0LFR9_SYNFM

ID   A0LFR9_SYNFM            Unreviewed;       552 AA.
AC   A0LFR9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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   OrderedLocusNames=Sfum_0572 {ECO:0000313|EMBL:ABK16271.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16271.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16271.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK16271.1; -; Genomic_DNA.
DR   RefSeq; WP_011697444.1; NC_008554.1.
DR   STRING; 335543.Sfum_0572; -.
DR   EnsemblBacteria; ABK16271; ABK16271; Sfum_0572.
DR   KEGG; sfu:Sfum_0572; -.
DR   eggNOG; ENOG4105C4K; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   eggNOG; COG0388; LUCA.
DR   HOGENOM; HOG000226694; -.
DR   KO; K01950; -.
DR   OMA; CEDIWND; -.
DR   OrthoDB; 1152435at2; -.
DR   BioCyc; SFUM335543:G1G7I-587-MONOMER; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-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; 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; 2.
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;
DR   PRODOM; A0LFR9.
DR   SWISS-2DPAGE; A0LFR9.
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:UP000001784};
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:UP000001784}.
FT   DOMAIN        1    255       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
FT   NP_BIND     294    301       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE     41     41       Proton acceptor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10139}.
FT   ACT_SITE     41     41       Proton acceptor; for glutaminase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   ACT_SITE    112    112       For glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   ACT_SITE    148    148       Nucleophile; for glutaminase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     118    118       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     185    185       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     191    191       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     377    377       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     401    401       ATP. {ECO:0000256|HAMAP-Rule:MF_02090}.
FT   BINDING     406    406       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
FT   BINDING     516    516       Deamido-NAD. {ECO:0000256|HAMAP-Rule:
FT                                MF_02090}.
SQ   SEQUENCE   552 AA;  60972 MW;  2265C82C6A0111C7 CRC64;
     MRIAIGQIDP FIGDFKGNAA KICDGVDRAR REGCDLVVFP EMALIGYPPR DLLDKPSFVR
     TSREHWEAIR EASRGIGVIF GAVDENPNGT GKPYHNAAVF FDDGKPAAIA HKMLLPSYDV
     FDEERYFEPG KHATWVDFRG ERLGITICED VWNVPRFLPR RLYHCDPIRE LEQASVSVIV
     NISASPYHVG KASYVGELLR SHAQRSGTQV IYVNQVGGND ELIFHGHSMV WDEAGKLVAS
     AADFREDFVV YDTRTHAGKL HAVGGDQAEE VIEALVLGLR DYVRKNRFGK AVVGLSGGVD
     SALTVCLAVL ALGAENVLGV GMPGPFNAPE SLEDAKELAR RLGIAFETVP IGDLFDAALR
     TLAPPFHGQP RDVTEENLQA RIRGMILMAI SNKFNRILLS TGNKSEIAVG YCTLYGDMNG
     GLSVLGDVPK TMVYELARKL NAQHDWIPER TLVRAPSAEL RPDQTDQDTL PPYEVLDAIL
     ADYVEKRLPA EEIASHGWDA ALVKWVTDRV DCNEYKRWQA PPILRVTTKA FGMGRRNPIA
     HGYREGGARQ CS
//

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