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Protein

FAD:protein FMN transferase

Gene

apbE

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Displays FAD pyrophosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (PubMed:23447540).By similarity1 Publication

Catalytic activityi

FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP.By similarity

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Magnesium. Can also use manganese.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811FAD1 Publication
Metal bindingi184 – 1841Magnesium; via carbonyl oxygen1 Publication
Binding sitei187 – 1871FAD1 Publication
Metal bindingi306 – 3061Magnesium1 Publication
Metal bindingi310 – 3101Magnesium1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi118 – 1203FAD1 Publication
Nucleotide bindingi278 – 2803FAD1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciTPAL243276:GC1H-844-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD:protein FMN transferaseBy similarity (EC:2.7.1.180By similarity)
Alternative name(s):
Flavin transferaseBy similarity
Gene namesi
Name:apbE
Ordered Locus Names:TP_0796
OrganismiTreponema pallidum (strain Nichols)
Taxonomic identifieri243276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000000811 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane PROSITE-ProRule annotationBy similarity; Lipid-anchor PROSITE-ProRule annotationBy similarity; Periplasmic side By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222PROSITE-ProRule annotationAdd
BLAST
Chaini23 – 362340FAD:protein FMN transferasePRO_0000001751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi23 – 231N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi23 – 231S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi243276.TP0796.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 389Combined sources
Beta strandi41 – 499Combined sources
Helixi53 – 7422Combined sources
Beta strandi79 – 813Combined sources
Helixi82 – 887Combined sources
Turni89 – 913Combined sources
Beta strandi95 – 973Combined sources
Helixi99 – 11416Combined sources
Turni115 – 1173Combined sources
Helixi124 – 13512Combined sources
Helixi142 – 1498Combined sources
Helixi154 – 1563Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi169 – 1735Combined sources
Turni183 – 1853Combined sources
Helixi186 – 20015Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 26315Combined sources
Beta strandi266 – 2716Combined sources
Beta strandi274 – 2785Combined sources
Turni282 – 2843Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi293 – 3008Combined sources
Helixi302 – 31514Combined sources
Helixi317 – 3248Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi339 – 3435Combined sources
Turni345 – 3473Combined sources
Helixi348 – 3503Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi358 – 3603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFUX-ray1.83A23-362[»]
4IFWX-ray2.30A23-362[»]
4IFXX-ray1.45A23-362[»]
4IFZX-ray1.90A23-362[»]
4IG1X-ray1.43A23-362[»]
ProteinModelPortaliO83774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ApbE family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1477.
KOiK03734.
OMAiRVYSYSA.
OrthoDBiEOG6CGCF7.

Family and domain databases

InterProiIPR024932. ApbE.
IPR003374. ApbE-like.
[Graphical view]
PANTHERiPTHR30040:SF2. PTHR30040:SF2. 1 hit.
PfamiPF02424. ApbE. 1 hit.
[Graphical view]
PIRSFiPIRSF006268. ApbE. 1 hit.
SUPFAMiSSF143631. SSF143631. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O83774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSCVYWRI GVLVCILCGV GSCGGRARVR EYSRAELVIG TLCRVRVYSK
60 70 80 90 100
RPAAEVHAAL EEVFTLLQQQ EMVLSANRDD SALAALNAQA GSAPVVVDRS
110 120 130 140 150
LYALLERALF FAEKSGGAFN PALGAXVKLW NIGFDRAAVP DPDALKEALT
160 170 180 190 200
RCDFRQVHLR AGVSVGAPHT VQLAQAGMQL DLGAIAKGFL ADKIVQLLTA
210 220 230 240 250
HALDSALVDL GGNIFALGLK YGDVRSAAAQ RLEWNVGIRD PHGTGQKPAL
260 270 280 290 300
VVSVRDCSVV TSGAYERFFE RDGVRYHHII DPVTGFPAHT DVDSVSIFAP
310 320 330 340 350
RSTDADALAT ACFVLGYEKS CALLREFPGV DALFIFPDKR VRASAGIVDR
360
VRVLDARFVL ER
Length:362
Mass (Da):39,064
Last modified:November 1, 1998 - v1
Checksum:iE64E2FAFD1A7041C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65759.1.
PIRiC71281.
RefSeqiWP_010882241.1. NC_000919.1.

Genome annotation databases

EnsemblBacteriaiAAC65759; AAC65759; TP_0796.
GeneIDi2610802.
KEGGitpa:TP0796.
PATRICi20531687. VBITrePal57110_0841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65759.1.
PIRiC71281.
RefSeqiWP_010882241.1. NC_000919.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFUX-ray1.83A23-362[»]
4IFWX-ray2.30A23-362[»]
4IFXX-ray1.45A23-362[»]
4IFZX-ray1.90A23-362[»]
4IG1X-ray1.43A23-362[»]
ProteinModelPortaliO83774.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243276.TP0796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC65759; AAC65759; TP_0796.
GeneIDi2610802.
KEGGitpa:TP0796.
PATRICi20531687. VBITrePal57110_0841.

Phylogenomic databases

eggNOGiCOG1477.
KOiK03734.
OMAiRVYSYSA.
OrthoDBiEOG6CGCF7.

Enzyme and pathway databases

BioCyciTPAL243276:GC1H-844-MONOMER.

Family and domain databases

InterProiIPR024932. ApbE.
IPR003374. ApbE-like.
[Graphical view]
PANTHERiPTHR30040:SF2. PTHR30040:SF2. 1 hit.
PfamiPF02424. ApbE. 1 hit.
[Graphical view]
PIRSFiPIRSF006268. ApbE. 1 hit.
SUPFAMiSSF143631. SSF143631. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nichols.
  2. "The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis."
    Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V.
    J. Biol. Chem. 288:11106-11121(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 23-362 IN COMPLEXES WITH ADP; AMP; FAD AND MAGNESIUM, FUNCTION, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiAPBE_TREPA
AccessioniPrimary (citable) accession number: O83774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: July 22, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.