UniProtKB - P0AB85 (APBE_ECOLI)
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Protein
FAD:protein FMN transferase
Gene
apbE
Organism
Escherichia coli (strain K12)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 42 | FAD; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 79 | FADBy similarity | 1 | |
Binding sitei | 182 | FADBy similarity | 1 | |
Metal bindingi | 185 | Magnesium; via carbonyl oxygenCurated1 Publication | 1 | |
Binding sitei | 188 | FADBy similarity | 1 | |
Binding sitei | 273 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 299 | MagnesiumCurated1 Publication | 1 | |
Metal bindingi | 302 | MagnesiumCurated1 Publication | 1 | |
Metal bindingi | 303 | MagnesiumCurated1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 120 – 122 | FADBy similarity | 3 |
GO - Molecular functioni
- FAD binding Source: EcoCyc
- metal ion binding Source: EcoCyc
- transferase activity Source: EcoCyc
GO - Biological processi
- protein flavinylation Source: EcoCyc
Keywordsi
Molecular function | Transferase |
Ligand | FAD, Flavoprotein, Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc: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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Organism-specific databases
EcoGenei | EG12073. apbE. |
Subcellular locationi
- Cell inner membrane PROSITE-ProRule annotationBy similarity; Lipid-anchor PROSITE-ProRule annotationBy similarity; Periplasmic side By similarity
GO - Cellular componenti
- intrinsic component of periplasmic side of plasma membrane Source: EcoCyc
- outer membrane-bounded periplasmic space Source: EcoCyc
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | PROSITE-ProRule annotationAdd BLAST | 19 | |
ChainiPRO_0000001748 | 20 – 351 | FAD:protein FMN transferaseAdd BLAST | 332 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 20 | N-palmitoyl cysteinePROSITE-ProRule annotation | 1 | |
Lipidationi | 20 | S-diacylglycerol cysteinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Lipoprotein, PalmitateProteomic databases
PaxDbi | P0AB85. |
PRIDEi | P0AB85. |
Interactioni
Subunit structurei
Homodimer.1 Publication
Protein-protein interaction databases
BioGridi | 4261922. 69 interactors. |
STRINGi | 316385.ECDH10B_2371. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 34 – 41 | Combined sources | 8 | |
Beta strandi | 44 – 52 | Combined sources | 9 | |
Helixi | 55 – 76 | Combined sources | 22 | |
Beta strandi | 78 – 80 | Combined sources | 3 | |
Helixi | 84 – 90 | Combined sources | 7 | |
Beta strandi | 97 – 99 | Combined sources | 3 | |
Helixi | 101 – 116 | Combined sources | 16 | |
Turni | 117 – 119 | Combined sources | 3 | |
Helixi | 126 – 132 | Combined sources | 7 | |
Helixi | 146 – 153 | Combined sources | 8 | |
Helixi | 158 – 160 | Combined sources | 3 | |
Beta strandi | 161 – 165 | Combined sources | 5 | |
Beta strandi | 170 – 176 | Combined sources | 7 | |
Turni | 184 – 186 | Combined sources | 3 | |
Helixi | 187 – 201 | Combined sources | 15 | |
Beta strandi | 206 – 211 | Combined sources | 6 | |
Beta strandi | 214 – 220 | Combined sources | 7 | |
Beta strandi | 224 – 226 | Combined sources | 3 | |
Beta strandi | 229 – 231 | Combined sources | 3 | |
Beta strandi | 243 – 245 | Combined sources | 3 | |
Beta strandi | 251 – 256 | Combined sources | 6 | |
Turni | 259 – 262 | Combined sources | 4 | |
Turni | 275 – 277 | Combined sources | 3 | |
Beta strandi | 278 – 280 | Combined sources | 3 | |
Beta strandi | 285 – 294 | Combined sources | 10 | |
Helixi | 295 – 308 | Combined sources | 14 | |
Helixi | 310 – 320 | Combined sources | 11 | |
Beta strandi | 323 – 329 | Combined sources | 7 | |
Beta strandi | 334 – 338 | Combined sources | 5 | |
Helixi | 340 – 343 | Combined sources | 4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2O18 | X-ray | 2.20 | A/B/C/D | 21-351 | [»] | |
4XGV | X-ray | 1.88 | A/B/C/D | 21-351 | [»] | |
4XGW | X-ray | 1.75 | A/B/C/D | 21-351 | [»] | |
4XGX | X-ray | 1.90 | A/B | 21-351 | [»] | |
ProteinModelPortali | P0AB85. | |||||
SMRi | P0AB85. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AB85. |
Family & Domainsi
Sequence similaritiesi
Belongs to the ApbE family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG4105CJ2. Bacteria. COG1477. LUCA. |
HOGENOMi | HOG000080808. |
InParanoidi | P0AB85. |
KOi | K03734. |
OMAi | MGTFWRV. |
PhylomeDBi | P0AB85. |
Family and domain databases
InterProi | View protein in InterPro IPR024932. ApbE. IPR003374. ApbE-like_sf. |
PANTHERi | PTHR30040. PTHR30040. 1 hit. |
Pfami | View protein in Pfam PF02424. ApbE. 1 hit. |
PIRSFi | PIRSF006268. ApbE. 1 hit. |
SUPFAMi | SSF143631. SSF143631. 1 hit. |
PROSITEi | View protein in PROSITE PS51257. PROKAR_LIPOPROTEIN. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0AB85-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | D64991. |
RefSeqi | NP_416718.1. NC_000913.3. WP_000406064.1. NZ_LN832404.1. |
Genome annotation databases
EnsemblBacteriai | AAC75274; AAC75274; b2214. BAA15997; BAA15997; BAA15997. |
GeneIDi | 946711. |
KEGGi | ecj:JW5368. eco:b2214. |
PATRICi | fig|1411691.4.peg.21. |
Similar proteinsi
Entry informationi
Entry namei | APBE_ECOLI | |
Accessioni | P0AB85Primary (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 28, 2018 | |
This is version 93 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |