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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)DescriptionActionsGraphical viewLength
Binding sitei181FAD1 Publication1
Metal bindingi184Magnesium; via carbonyl oxygen1 Publication1
Binding sitei187FAD1 Publication1
Metal bindingi306Magnesium1 Publication1
Metal bindingi310Magnesium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi118 – 120FAD1 Publication3
Nucleotide bindingi278 – 280FAD1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding

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
Proteomesi
  • UP000000811 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22PROSITE-ProRule annotationAdd BLAST22
ChainiPRO_000000175123 – 362FAD:protein FMN transferaseAdd BLAST340

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi23N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi23S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi243276.TP0796.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 38Combined sources9
Beta strandi41 – 49Combined sources9
Helixi53 – 74Combined sources22
Beta strandi79 – 81Combined sources3
Helixi82 – 88Combined sources7
Turni89 – 91Combined sources3
Beta strandi95 – 97Combined sources3
Helixi99 – 114Combined sources16
Turni115 – 117Combined sources3
Helixi124 – 136Combined sources13
Helixi142 – 149Combined sources8
Helixi154 – 156Combined sources3
Beta strandi157 – 161Combined sources5
Beta strandi169 – 173Combined sources5
Turni183 – 185Combined sources3
Helixi186 – 200Combined sources15
Beta strandi206 – 210Combined sources5
Beta strandi213 – 218Combined sources6
Beta strandi234 – 239Combined sources6
Beta strandi245 – 263Combined sources19
Beta strandi266 – 271Combined sources6
Beta strandi274 – 278Combined sources5
Turni282 – 284Combined sources3
Beta strandi285 – 287Combined sources3
Beta strandi293 – 300Combined sources8
Helixi302 – 315Combined sources14
Helixi317 – 324Combined sources8
Beta strandi331 – 335Combined sources5
Beta strandi339 – 343Combined sources5
Turni345 – 347Combined sources3
Helixi348 – 350Combined sources3
Beta strandi351 – 355Combined sources5
Beta strandi358 – 360Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IFUX-ray1.83A23-362[»]
4IFWX-ray2.30A23-362[»]
4IFXX-ray1.45A23-362[»]
4IFZX-ray1.90A23-362[»]
4IG1X-ray1.43A23-362[»]
4XDRX-ray1.40A23-362[»]
4XDTX-ray1.45A23-362[»]
4XDUX-ray1.35A23-362[»]
ProteinModelPortaliO83774.
SMRiO83774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ApbE family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CJ2. Bacteria.
COG1477. LUCA.
KOiK03734.
OMAiINIKAYG.

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:TP_0796.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IFUX-ray1.83A23-362[»]
4IFWX-ray2.30A23-362[»]
4IFXX-ray1.45A23-362[»]
4IFZX-ray1.90A23-362[»]
4IG1X-ray1.43A23-362[»]
4XDRX-ray1.40A23-362[»]
4XDTX-ray1.45A23-362[»]
4XDUX-ray1.35A23-362[»]
ProteinModelPortaliO83774.
SMRiO83774.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243276.TP0796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CJ2. Bacteria.
COG1477. LUCA.
KOiK03734.
OMAiINIKAYG.

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...

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: November 2, 2016
This is version 92 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

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 one 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.