SPM_003580
  | Uniprot: A0A037UR91
Description: NAD synthetase EC number: 6.3.1.5 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + diphosphate + NAD(+). {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00016647}. Cofactor: Enzyme regulation: Function [CC]: Pathway: PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|SAAS:SAAS00016631}. Active site: ACT_SITE 32 32 {ECO:0000256|HAMAP-Rule:MF_00193}. Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 30 37 ATP. {ECO:0000256|HAMAP-Rule:MF_00193}. Site: Gene names (primary): nadE Gene names (synonym): Mass: 27,661 Subunit structure [CC]: Gene ontology (GO): ATP binding [GO:0005524]; NAD+ synthase (glutamine-hydrolyzing) activity [GO:0003952]; NAD+ synthase activity [GO:0008795]; NAD biosynthetic process [GO:0009435] Gene ontology IDs: GO:0003952; GO:0005524; GO:0008795; GO:0009435 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00541228}. Protein families: NAD synthetase family Coiled coil: Domain [FT]: DOMAIN 8 233 NAD_synthase. {ECO:0000259|Pfam:PF02540}. Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: A0A037UR91 MEROPS: EnsemblBacteria KO: KAI93058 UniPathway: CDD: Gene3D: cd00553 HAMAP: 3.40.50.620 InterPro: MF_00193 PANTHER: IPR022310;IPR003694;IPR022926;IPR014729 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF02540 SMART: SUPFAM: TIGRFAMs: |
676964-677714(+) >nucleotide sequence AAAGCCCACTGCCAAGGGGTTATTGTCGGTTTATCAGGTGGAATTGATTCGGCTGTTGTT AGTTTATTAGCAAAACAAGCTTTTCCTGAGCAACATTTAACAGTTATAATGCCTTGTCAT TCTGACTATTTTGATCAAGAATGTGCACAGTTGTTAGTTAATAATCATCAATTAAAAAAT CATCTTGTTGATTTAACAGGAACATATGATAATTTAATTGCAACATTAGCTTTGCCACCT CATCAATTAGCATTCGCTAATATAAAGCCACGGTTACGAATGACAACCTTATATGCTTTA GCACAAAGTCACAATTATATGGTTTTAGGAACGGATAATGCTGATGAATGACATGTCGGA TATTTTACTAAATATGGTGATGGTGCTGCTGATTTAGTCCCTATTATTCATTTACTAAAA TCGGAAGTTCAGCAAGCAGCACAATTATTAGGTGTGCCATCAGCAATTATTTCACGTCCA CCAACAGCGGGATTATGAGCTAGTCAAACTGATGAAAAAGAATTAGGGTTTACTTATCAA CAATTAGATTATTATTTACAAGGAAAATCAGTTCCAACAGCGATTGCACAACGAATTAAA CAATTAAATCAAAGTTCTGAACATAAACGACATTTACCTAAAGCACCACCAAATATTTTT AGTTCGTTAATTTCTGTTAGTAAAGATTAA >protein sequence SDYFDQECAQLLVNNHQLKNHLVDLTGTYDNLIATLALPPHQLAFANIKPRLRMTTLYAL AQSHNYMVLGTDNADEWHVGYFTKYGDGAADLVPIIHLLKSEVQQAAQLLGVPSAIISRP PTAGLWASQTDEKELGFTYQQLDYYLQGKSVPTAIAQRIKQLNQSSEHKRHLPKAPPNIF SSLISVSKD |
© Fisunov Lab of Proteomics, 2016.