APBE1_KLEP3
ID APBE1_KLEP3 Reviewed; 350 AA.
AC B5XP00;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=FAD:protein FMN transferase {ECO:0000303|PubMed:23558683};
DE EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3};
DE AltName: Full=Flavin transferase {ECO:0000303|PubMed:23558683};
DE Flags: Precursor;
GN Name=apbE1 {ECO:0000303|PubMed:23558683};
GN Synonyms=apbE {ECO:0000312|EMBL:ACI11195.1};
GN OrderedLocusNames=KPK_1517 {ECO:0000312|EMBL:ACI11195.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=204;
RX PubMed=23558683; DOI=10.1074/jbc.m113.455402;
RA Bertsova Y.V., Fadeeva M.S., Kostyrko V.A., Serebryakova M.V., Baykov A.A.,
RA Bogachev A.V.;
RT "Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase
RT catalyzing covalent attachment of FMN to a threonine residue in bacterial
RT flavoproteins.";
RL J. Biol. Chem. 288:14276-14286(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=204;
RX PubMed=24361839; DOI=10.1016/j.bbabio.2013.12.006;
RA Bertsova Y.V., Kostyrko V.A., Baykov A.A., Bogachev A.V.;
RT "Localization-controlled specificity of FAD:threonine flavin transferases
RT in Klebsiella pneumoniae and its implications for the mechanism of Na(+)-
RT translocating NADH:quinone oxidoreductase.";
RL Biochim. Biophys. Acta 1837:1122-1129(2014).
CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the FMN
CC moiety of FAD and its covalent binding to the hydroxyl group of a
CC threonine residue in a target flavoprotein such as NqrB and NqrC, two
CC subunits of the NQR complex. {ECO:0000250|UniProtKB:A5F5Y3,
CC ECO:0000269|PubMed:24361839, ECO:0000303|PubMed:23558683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] +
CC H(+); Xref=Rhea:RHEA:36847, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11061, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:74257, ChEBI:CHEBI:456215; EC=2.7.1.180;
CC Evidence={ECO:0000250|UniProtKB:A5F5Y3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5F5Y3};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303};
CC Lipid-anchor {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P41780,
CC ECO:0000269|PubMed:24361839}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene results in a complete
CC loss of the quinone reductase activity of the Na(+)-NQR complex, but
CC does not affect the NADH dehydrogenase activity. Cytoplasmic fumarate
CC reductase activity displayed by KPK_2907, which contains a covalently
CC bound FMN, remains unchanged in mutant cells.
CC {ECO:0000269|PubMed:23558683, ECO:0000269|PubMed:24361839}.
CC -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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DR EMBL; CP000964; ACI11195.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XP00; -.
DR SMR; B5XP00; -.
DR EnsemblBacteria; ACI11195; ACI11195; KPK_1517.
DR KEGG; kpe:KPK_1517; -.
DR HOGENOM; CLU_044403_0_0_6; -.
DR OMA; MGTFWRV; -.
DR OrthoDB; 2021063at2; -.
DR BRENDA; 2.7.1.180; 2814.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017013; P:protein flavinylation; IDA:CACAO.
DR Gene3D; 3.10.520.10; -; 1.
DR InterPro; IPR024932; ApbE.
DR InterPro; IPR003374; ApbE-like_sf.
DR PANTHER; PTHR30040; PTHR30040; 1.
DR Pfam; PF02424; ApbE; 1.
DR PIRSF; PIRSF006268; ApbE; 1.
DR SUPFAM; SSF143631; SSF143631; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Palmitate; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..350
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000430776"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 119..121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 350 AA; 37831 MW; 517869560292343A CRC64;
MDMTFFRAAL LGACVLLSGC DSATTPASPA STATVLDGKT MGTFWRVSVI GVDEAKAEAL
RAKVQAQLDA DDRLLSTWKN DSALMRFNHA ADTRPWPVSE AMVDIVTLSL RIGAKTHGAM
DITVGPLVNL WGFGPDKQPV TTPDAQAIAA AKARTGLQHL QVINQSGRQF LQKDIPDLFV
DLSTVGEGYA ADHLARLMEQ EGISRYLVSV GGALVSRGMN GEGKPWRVAI QKPTDRENAV
QAIVDINGHG ISTSGSYRNY YELDGKRISH VIDPQTGQPI THKLVSVTVI APTALEADGW
DTGLMVLGPE KAQQVVREQG LAVYMIVKEG EGFKTWMSPQ FRTFLVGEKN
