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
ATGAAAAAAATATGGGCAGTTATCAACTTAATATTAATCAGTGTTCTTTTTTCTGCTTGT
ACACAACAAGCAATTGATAACAGTTTAGCCATATCATCTATGGATACATTTATTGGTGGC
ACAGTACATGCACCAAAAGCTGTTTGGGATAAAGCGGATAAAAAACTAAAAGAAATGTAT
ATGCTCTACCACGAGTTAACCGATAACTATAGAGGTTATGAGGGTGTACAAGGTGTTTAC
TATATTAATAATTTAGTAGAAACAACGAAAACTGACCAAACAGTTGAGATTAAAAAAGAA
CTTTATGATCTATTAAGTTTAGGTGTAGAACTCTATGAATTTACAGATGGATACTTTGAT
ATGTCCATTGGTAAGATCATCGATGTTTGGAAAAACTTAATTGATGAAAGTGATTATACG
GGTCAAGAAATACCTAAAGAAGATATCGATTATGCGATAAACTTAGTGGATGCTATTGAT
ATCATTGAAGATCCGGTGATTTTAAGTGAAGTAGATAATAAATATTACGTGACACTTAAA
TATGGTGCAAAACTAGACTTAGGTGCGCTTGCTAAAGGGTATGTCACTCAGTTAGCAGCA
GATTATTTAACGGATTTAGGTTTAAGTACCTATCTCATTAGTGGTGGTGGCTCATCCATG
TTATATGGTGAAGGTAATCCAAAAACTGAAGATGGTAGTTACAGAACAGGACTTATTAAT
CCACAAGATGTTATTGATAACTTAGATATTATTGGATATCGACCTAAAAATTACGGTATA
TATACAGCTAAAAATTATAACTTCACAACATCAGGAAGTTATAATCAATTTATCTTAAGT
GAAGGTGTGATGTATCATCACATTGTCTCACCTAAAACAAAACGTCCGGTAAATCATTAT
CTAACACTTTCTATTGTTGGAACAGATGCAGGATTTAATGATGGTTTATCCACAGCATTA
TTTAGTATGCCACCTGAAGTGTTAGAACAGTTTTTAGAAACGAATGGTTATGAGGTCTAT
ACATATTTATTTAATAATACTTATAAATCCTATAATCAATCTGAAAACTTTAGACCACTT
TAA


>protein sequence
MKKIWAVINLILISVLFSACTQQAIDNSLAISSMDTFIGGTVHAPKAVWDKADKKLKEMY
MLYHELTDNYRGYEGVQGVYYINNLVETTKTDQTVEIKKELYDLLSLGVELYEFTDGYFD
MSIGKIIDVWKNLIDESDYTGQEIPKEDIDYAINLVDAIDIIEDPVILSEVDNKYYVTLK
YGAKLDLGALAKGYVTQLAADYLTDLGLSTYLISGGGSSMLYGEGNPKTEDGSYRTGLIN
PQDVIDNLDIIGYRPKNYGIYTAKNYNFTTSGSYNQFILSEGVMYHHIVSPKTKRPVNHY
LTLSIVGTDAGFNDGLSTALFSMPPEVLEQFLETNGYEVYTYLFNNTYKSYNQSENFRPL






















© Fisunov Lab of Proteomics, 2016.