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UniProtKB - P0AB85 (APBE_ECOLI)

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Protein

FAD:protein FMN transferase

Gene

apbE

Organism
Escherichia coli (strain K12)
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 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

  • FAD binding Source: EcoCyc
  • metal ion binding Source: EcoCyc
  • transferase activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  • protein flavinylation Source: EcoCyc
Complete GO annotation...

Keywordsi

Molecular functionTransferase
LigandFAD, Flavoprotein, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12073-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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
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.
STRINGi316385.ECDH10B_2371.

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.
PhylomeDBiP0AB85.

Family and domain databases

InterProiView protein in InterPro
IPR024932. ApbE.
IPR003374. ApbE-like.
PANTHERiPTHR30040. PTHR30040. 1 hit.
PfamiView protein in Pfam
PF02424. ApbE. 1 hit.
PIRSFiPIRSF006268. ApbE. 1 hit.
SUPFAMiSSF143631. SSF143631. 1 hit.
PROSITEiView protein in PROSITE
PS51257. PROKAR_LIPOPROTEIN. 1 hit.

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.
PATRICifig|1411691.4.peg.21.

Similar proteinsi

Entry informationi

Entry nameiAPBE_ECOLI
AccessioniPrimary (citable) accession number: P0AB85
Secondary accession number(s): P33943, P33944, P76455
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: August 30, 2017
This is version 90 of the entry and version 1 of the sequence. See 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