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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421FAD; via carbonyl oxygenBy similarity
Binding sitei79 – 791FADBy similarity
Binding sitei182 – 1821FADBy similarity
Metal bindingi185 – 1851Magnesium; via carbonyl oxygenCurated1 Publication
Binding sitei188 – 1881FADBy similarity
Binding sitei273 – 2731FAD; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi299 – 2991MagnesiumCurated1 Publication
Metal bindingi302 – 3021MagnesiumCurated1 Publication
Metal bindingi303 – 3031MagnesiumCurated1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1223FADBy similarity

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919PROSITE-ProRule annotationAdd
BLAST
Chaini20 – 351332FAD:protein FMN transferasePRO_0000001748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi20 – 201N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi20 – 201S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0AB85.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4261922. 14 interactions.
STRINGi511145.b2214.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 418Combined sources
Beta strandi44 – 529Combined sources
Helixi55 – 7622Combined sources
Beta strandi78 – 803Combined sources
Helixi84 – 907Combined sources
Beta strandi97 – 993Combined sources
Helixi101 – 11616Combined sources
Turni117 – 1193Combined sources
Helixi126 – 1327Combined sources
Helixi146 – 1538Combined sources
Helixi158 – 1603Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi170 – 1767Combined sources
Turni184 – 1863Combined sources
Helixi187 – 20115Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi214 – 2207Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi251 – 2566Combined sources
Turni259 – 2624Combined sources
Turni275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi285 – 29410Combined sources
Helixi295 – 30814Combined sources
Helixi310 – 32011Combined sources
Beta strandi323 – 3297Combined sources
Beta strandi334 – 3385Combined sources
Helixi340 – 3434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 32-349.
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.
OrthoDBiEOG6CGCF7.
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 AAA16404.1 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
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. Positions 32-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261922. 14 interactions.
STRINGi511145.b2214.

Proteomic databases

PaxDbiP0AB85.

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.
OrthoDBiEOG6CGCF7.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "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: SUBUNIT.
  6. "Crystal structure of a thiamine biosynthesis lipoprotein ApbE."
    Northeast structural genomics consortium (NESG)
    Submitted (NOV-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-351 IN COMPLEX WITH CALCIUM.

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: March 16, 2016
This is version 82 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.