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Protein

FAD:protein FMN transferase

Gene

apbE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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 such as NqrB and NqrC, two subunits of the NQR complex.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42FAD; via carbonyl oxygenBy similarity1
Binding sitei79FADBy similarity1
Binding sitei182FADBy similarity1
Metal bindingi185Magnesium; via carbonyl oxygenCurated1 Publication1
Binding sitei188FADBy similarity1
Binding sitei273FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi299MagnesiumCurated1 Publication1
Metal bindingi302MagnesiumCurated1 Publication1
Metal bindingi303MagnesiumCurated1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi120 – 122FADBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12073-MONOMER.
ECOL316407:JW5368-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
Synonyms:yojK, yojL
Ordered Locus Names:b2214, JW5368
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12073. apbE.

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 – 19PROSITE-ProRule annotationAdd BLAST19
ChainiPRO_000000174820 – 351FAD:protein FMN transferaseAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi20N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi20S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0AB85.
PRIDEiP0AB85.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4261922. 14 interactors.
STRINGi511145.b2214.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 41Combined sources8
Beta strandi44 – 52Combined sources9
Helixi55 – 76Combined sources22
Beta strandi78 – 80Combined sources3
Helixi84 – 90Combined sources7
Beta strandi97 – 99Combined sources3
Helixi101 – 116Combined sources16
Turni117 – 119Combined sources3
Helixi126 – 132Combined sources7
Helixi146 – 153Combined sources8
Helixi158 – 160Combined sources3
Beta strandi161 – 165Combined sources5
Beta strandi170 – 176Combined sources7
Turni184 – 186Combined sources3
Helixi187 – 201Combined sources15
Beta strandi206 – 211Combined sources6
Beta strandi214 – 220Combined sources7
Beta strandi224 – 226Combined sources3
Beta strandi229 – 231Combined sources3
Beta strandi243 – 245Combined sources3
Beta strandi251 – 256Combined sources6
Turni259 – 262Combined sources4
Turni275 – 277Combined sources3
Beta strandi278 – 280Combined sources3
Beta strandi285 – 294Combined sources10
Helixi295 – 308Combined sources14
Helixi310 – 320Combined sources11
Beta strandi323 – 329Combined sources7
Beta strandi334 – 338Combined sources5
Helixi340 – 343Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O18X-ray2.20A/B/C/D21-351[»]
4XGVX-ray1.88A/B/C/D21-351[»]
4XGWX-ray1.75A/B/C/D21-351[»]
4XGXX-ray1.90A/B21-351[»]
ProteinModelPortaliP0AB85.
SMRiP0AB85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB85.

Family & Domainsi

Sequence similaritiesi

Belongs to the ApbE family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CJ2. Bacteria.
COG1477. LUCA.
HOGENOMiHOG000080808.
InParanoidiP0AB85.
KOiK03734.
OMAiMGTFWRV.
PhylomeDBiP0AB85.

Family and domain databases

InterProiIPR024932. ApbE.
IPR003374. ApbE-like.
[Graphical view]
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.

P0AB85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEISFTRVAL LAAALFFVGC DQKPQPAKTH ATEVTVLEGK TMGTFWRASI
60 70 80 90 100
PGIDAKRSAE LKEKIQTQLD ADDQLLSTYK KDSALMRFND SQSLSPWPVS
110 120 130 140 150
EAMADIVTTS LRIGAKTDGA MDITVGPLVN LWGFGPEQQP VQIPSQEQID
160 170 180 190 200
AMKAKTGLQH LTVINQSHQQ YLQKDLPDLY VDLSTVGEGY AADHLARLME
210 220 230 240 250
QEGISRYLVS VGGALNSRGM NGEGLPWRVA IQKPTDKENA VQAVVDINGH
260 270 280 290 300
GISTSGSYRN YYELDGKRLS HVIDPQTGRP IEHNLVSVTV IAPTALEADA
310 320 330 340 350
WDTGLMVLGP EKAKEVVRRE GLAVYMITKE GDSFKTWMSP QFKSFLVSEK

N
Length:351
Mass (Da):38,549
Last modified:November 8, 2005 - v1
Checksum:i53D370B6BFF843D2
GO

Sequence cautioni

The sequence AAA16404 differs from that shown. Reason: Frameshift at position 122. Produces two separate ORFs.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16405.1. Frameshift.
U00008 Genomic DNA. Translation: AAA16404.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75274.1.
AP009048 Genomic DNA. Translation: BAA15997.1.
PIRiD64991.
RefSeqiNP_416718.1. NC_000913.3.
WP_000406064.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75274; AAC75274; b2214.
BAA15997; BAA15997; BAA15997.
GeneIDi946711.
KEGGiecj:JW5368.
eco:b2214.
PATRICi32119787. VBIEscCol129921_2303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16405.1. Frameshift.
U00008 Genomic DNA. Translation: AAA16404.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75274.1.
AP009048 Genomic DNA. Translation: BAA15997.1.
PIRiD64991.
RefSeqiNP_416718.1. NC_000913.3.
WP_000406064.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O18X-ray2.20A/B/C/D21-351[»]
4XGVX-ray1.88A/B/C/D21-351[»]
4XGWX-ray1.75A/B/C/D21-351[»]
4XGXX-ray1.90A/B21-351[»]
ProteinModelPortaliP0AB85.
SMRiP0AB85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261922. 14 interactors.
STRINGi511145.b2214.

Proteomic databases

PaxDbiP0AB85.
PRIDEiP0AB85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75274; AAC75274; b2214.
BAA15997; BAA15997; BAA15997.
GeneIDi946711.
KEGGiecj:JW5368.
eco:b2214.
PATRICi32119787. VBIEscCol129921_2303.

Organism-specific databases

EchoBASEiEB1998.
EcoGeneiEG12073. apbE.

Phylogenomic databases

eggNOGiENOG4105CJ2. Bacteria.
COG1477. LUCA.
HOGENOMiHOG000080808.
InParanoidiP0AB85.
KOiK03734.
OMAiMGTFWRV.
PhylomeDBiP0AB85.

Enzyme and pathway databases

BioCyciEcoCyc:EG12073-MONOMER.
ECOL316407:JW5368-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AB85.
PROiP0AB85.

Family and domain databases

InterProiIPR024932. ApbE.
IPR003374. ApbE-like.
[Graphical view]
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_ECOLI
AccessioniPrimary (citable) accession number: P0AB85
Secondary accession number(s): P33943, P33944, P76455
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 85 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.