(data stored in ACNUC7421 zone)

SWISSPROT: NADE_PSEHT

ID   NADE_PSEHT              Reviewed;         278 AA.
AC   Q3IF87;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 77.
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};
GN   OrderedLocusNames=PSHAa0075;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to
CC       form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC       Rule:MF_00193}.
CC   -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP +
CC       diphosphate + NAD(+). {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.
CC       {ECO:0000255|HAMAP-Rule:MF_00193}.
DR   EMBL; CR954246; CAI85184.1; -; Genomic_DNA.
DR   RefSeq; WP_011326802.1; NC_007481.1.
DR   ProteinModelPortal; Q3IF87; -.
DR   SMR; Q3IF87; -.
DR   STRING; 326442.PSHAa0075; -.
DR   EnsemblBacteria; CAI85184; CAI85184; PSHAa0075.
DR   KEGG; pha:PSHAa0075; -.
DR   PATRIC; fig|326442.8.peg.74; -.
DR   eggNOG; ENOG4107RA1; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   HOGENOM; HOG000238070; -.
DR   KO; K01916; -.
DR   OMA; CAINPIG; -.
DR   OrthoDB; POG091H02ZG; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-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   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;
DR   PRODOM; Q3IF87.
DR   SWISS-2DPAGE; Q3IF87.
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; NAD;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    278       NH(3)-dependent NAD(+) synthetase.
FT                                /FTId=PRO_1000077584.
FT   NP_BIND      43     50       ATP. {ECO:0000255|HAMAP-Rule:MF_00193}.
FT   NP_BIND     266    267       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   METAL        49     49       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   METAL       171    171       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   BINDING     146    146       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   BINDING     166    166       ATP. {ECO:0000255|HAMAP-Rule:MF_00193}.
FT   BINDING     179    179       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   BINDING     186    186       Deamido-NAD. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
FT   BINDING     195    195       ATP. {ECO:0000255|HAMAP-Rule:MF_00193}.
FT   BINDING     217    217       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00193}.
SQ   SEQUENCE   278 AA;  30258 MW;  2405C23A2A614A3E CRC64;
     MRAEIMAAMK VQPVIDVNAE ISRRVNFIKA RLIAAHATSL VLGISGGVDS SVCGRLCQLA
     VNELNQEQST TDYKFVAVRL PYGVQADENE AQLAVDFIQP SSRMTVNIKP ATDALHEQTM
     AAIVGNGESL PEQEKIDFIK GNVKARQRMI AQYEIAAFCQ GLVVGTDHSA ENITGFYTKF
     GDGACDLAPL FGLSKRQVRA LGSTLGASSV LVNKAPTADL ESDRPGLTDE EALGLSYEQI
     DDFLEGKPVT QQVEQTLSAI YQRTQHKRQP VPTIYDEL
//

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