(data stored in ACNUC10043 zone)

SWISSPROT: D1YV70_METPS

ID   D1YV70_METPS            Unreviewed;       268 AA.
AC   D1YV70;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 55.
DE   RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812};
DE            EC=6.3.1.5 {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812};
GN   Name=nadE-1 {ECO:0000313|EMBL:BAI60342.1};
GN   Synonyms=nadE {ECO:0000256|HAMAP-Rule:MF_00193};
GN   OrderedLocusNames=MCP_0270 {ECO:0000313|EMBL:BAI60342.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60342.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC       NAD. Uses ammonia as a nitrogen source. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00193,
CC         ECO:0000256|RuleBase:RU003812};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00193, ECO:0000256|RuleBase:RU004252}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00193}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00193, ECO:0000256|RuleBase:RU003811}.
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DR   EMBL; AP011532; BAI60342.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0270; -.
DR   EnsemblBacteria; BAI60342; BAI60342; MCP_0270.
DR   KEGG; mpd:MCP_0270; -.
DR   PATRIC; fig|304371.9.peg.273; -.
DR   eggNOG; arCOG00069; Archaea.
DR   eggNOG; COG0171; LUCA.
DR   HOGENOM; HOG000238069; -.
DR   KO; K01916; -.
DR   OMA; CAINPIG; -.
DR   UniPathway; UPA00253; UER00333.
DR   Proteomes; UP000001882; 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;
DR   PRODOM; D1YV70.
DR   SWISS-2DPAGE; D1YV70.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|RuleBase:RU003811};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00193};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00193};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00193,
KW   ECO:0000256|RuleBase:RU003811};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   DOMAIN          16..257
FT                   /note="NAD_synthase"
FT                   /evidence="ECO:0000259|Pfam:PF02540"
FT   NP_BIND         37..44
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   NP_BIND         252..253
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   METAL           43
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   METAL           146
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         121
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         141
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         154
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         161
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         170
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
FT   BINDING         192
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00193"
SQ   SEQUENCE   268 AA;  29171 MW;  F559AE66A75466C3 CRC64;
     MKGLLLSKDE LVKCENAIEE SIVRAVETSK MNGAILALSG GIDSALVAVL ASRVVDVFGL
     LLPDRATSDP GDMEDARDLA KSLGMDYELI EIGGIVEAVY SARPNLGPKE CRLAYANVKP
     RVRMIMNYFA SNLDGRIVLG TGNKTELLMG YFTKYGDGGV DLLPIAGLYK TRVRQMAKHV
     GVPEAIIKKP PSAGLWKGQT DEGEMGISYE ALDKILYGVY DLGLSYGEIQ KETGVDEATF
     TRIMERVRDN EHKRNMPPIT DITAVIGP
//

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