ACL_RS00275
  | Uniprot: A9NEB6
Description: thiamine biosynthesis lipoprotein EC number: 2.7.1.180 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP. {ECO:0000256|RuleBase:RU363002}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; ; Note=Magnesium. Can also use manganese. {ECO:0000256|PIRSR:PIRSR006268-2} Enzyme regulation: Function [CC]: FUNCTION: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. {ECO:0000256|RuleBase:RU363002}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 189 189 Magnesium; via carbonyl oxygen. {ECO:0000256|PIRSR:PIRSR006268-2}.; METAL 314 314 Magnesium. {ECO:0000256|PIRSR:PIRSR006268-2}.; METAL 318 318 Magnesium. {ECO:0000256|PIRSR:PIRSR006268-2}. Nucleotide binding: Site: Gene names (primary): apbE Gene names (synonym): Mass: 40,587 Subunit structure [CC]: Gene ontology (GO): metal ion binding [GO:0046872]; transferase activity [GO:0016740]; protein flavinylation [GO:0017013] Gene ontology IDs: GO:0016740; GO:0017013; GO:0046872 Chain: CHAIN 25 360 FAD:protein FMN transferase. {ECO:0000256|RuleBase:RU363002}. /FTId=PRO_5005967830. Signal peptide: SIGNAL 1 24 {ECO:0000256|RuleBase:RU363002}. Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the ApbE family. {ECO:0000256|RuleBase:RU363002}. Protein families: ApbE family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NEB6 MEROPS: EnsemblBacteria KO: ABX80696 UniPathway: K03734 CDD: Gene3D: HAMAP: InterPro: PANTHER: IPR024932;IPR003374 PIRSF: PRINTS: PIRSF006268 PROSITE: Pfam: ProDom: PF02424 SMART: SUPFAM: TIGRFAMs: SSF143631 |
63790-64873(+) >nucleotide sequence ACACAACAAGCAATTGATAACAGTTTAGCCATATCATCTATGGATACATTTATTGGTGGC ACAGTACATGCACCAAAAGCTGTTTGGGATAAAGCGGATAAAAAACTAAAAGAAATGTAT ATGCTCTACCACGAGTTAACCGATAACTATAGAGGTTATGAGGGTGTACAAGGTGTTTAC TATATTAATAATTTAGTAGAAACAACGAAAACTGACCAAACAGTTGAGATTAAAAAAGAA CTTTATGATCTATTAAGTTTAGGTGTAGAACTCTATGAATTTACAGATGGATACTTTGAT ATGTCCATTGGTAAGATCATCGATGTTTGGAAAAACTTAATTGATGAAAGTGATTATACG GGTCAAGAAATACCTAAAGAAGATATCGATTATGCGATAAACTTAGTGGATGCTATTGAT ATCATTGAAGATCCGGTGATTTTAAGTGAAGTAGATAATAAATATTACGTGACACTTAAA TATGGTGCAAAACTAGACTTAGGTGCGCTTGCTAAAGGGTATGTCACTCAGTTAGCAGCA GATTATTTAACGGATTTAGGTTTAAGTACCTATCTCATTAGTGGTGGTGGCTCATCCATG TTATATGGTGAAGGTAATCCAAAAACTGAAGATGGTAGTTACAGAACAGGACTTATTAAT CCACAAGATGTTATTGATAACTTAGATATTATTGGATATCGACCTAAAAATTACGGTATA TATACAGCTAAAAATTATAACTTCACAACATCAGGAAGTTATAATCAATTTATCTTAAGT GAAGGTGTGATGTATCATCACATTGTCTCACCTAAAACAAAACGTCCGGTAAATCATTAT CTAACACTTTCTATTGTTGGAACAGATGCAGGATTTAATGATGGTTTATCCACAGCATTA TTTAGTATGCCACCTGAAGTGTTAGAACAGTTTTTAGAAACGAATGGTTATGAGGTCTAT ACATATTTATTTAATAATACTTATAAATCCTATAATCAATCTGAAAACTTTAGACCACTT TAA >protein sequence MLYHELTDNYRGYEGVQGVYYINNLVETTKTDQTVEIKKELYDLLSLGVELYEFTDGYFD MSIGKIIDVWKNLIDESDYTGQEIPKEDIDYAINLVDAIDIIEDPVILSEVDNKYYVTLK YGAKLDLGALAKGYVTQLAADYLTDLGLSTYLISGGGSSMLYGEGNPKTEDGSYRTGLIN PQDVIDNLDIIGYRPKNYGIYTAKNYNFTTSGSYNQFILSEGVMYHHIVSPKTKRPVNHY LTLSIVGTDAGFNDGLSTALFSMPPEVLEQFLETNGYEVYTYLFNNTYKSYNQSENFRPL |
© Fisunov Lab of Proteomics, 2016.