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NADE_PSESM
ID   NADE_PSESM              Reviewed;         275 AA.
AC   Q87VL4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193};
DE            EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193};
GN   Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193}; OrderedLocusNames=PSPTO_4922;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC       NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC       Rule:MF_00193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC         NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00193};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00193}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00193}.
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DR   EMBL; AE016853; AAO58350.1; -; Genomic_DNA.
DR   RefSeq; NP_794655.1; NC_004578.1.
DR   RefSeq; WP_005620808.1; NC_004578.1.
DR   AlphaFoldDB; Q87VL4; -.
DR   SMR; Q87VL4; -.
DR   STRING; 223283.PSPTO_4922; -.
DR   EnsemblBacteria; AAO58350; AAO58350; PSPTO_4922.
DR   GeneID; 61788226; -.
DR   KEGG; pst:PSPTO_4922; -.
DR   PATRIC; fig|223283.9.peg.5035; -.
DR   eggNOG; COG0171; Bacteria.
DR   HOGENOM; CLU_059327_3_0_6; -.
DR   OMA; MAFLYDY; -.
DR   OrthoDB; 1152435at2; -.
DR   PhylomeDB; Q87VL4; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
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   HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR003694; NAD_synthase.
DR   InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR23090; PTHR23090; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   TIGRFAMs; TIGR00552; nadE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..275
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152187"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         147
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         180
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         187
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         267..268
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
SQ   SEQUENCE   275 AA;  29870 MW;  38A2B2AFBA59C613 CRC64;
     MHAVQRQIAE QLKVQPPFAD QNALQAEVAR RVGFIKDCLQ NARLKTLVLG ISGGVDSLTA
     GLLAQRAVKE LRESTGDTRY RFIAVRLPYV VQADEHEAQA SVDFIEPDER HTINIGSSVK
     ALAAEVKAFD GLPASSVDFV LGNTKARMRM VAQYTVAGAY QGLVIGTDHA AEAVMGFFTK
     FGDGACDLAP LSGLVKNQVR AIARHFGAPE SLVEKVPTAD LEDLSPGKPD EASHGVTYAE
     IDAFLHGEPV REEAFRIICE TYAKTQHKRE LPYAP
 
 
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