APBE2_KLEP3
ID APBE2_KLEP3 Reviewed; 316 AA.
AC B5XRA9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=FAD:protein FMN transferase {ECO:0000250|UniProtKB:A5F5Y3};
DE EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3};
DE AltName: Full=Flavin transferase {ECO:0000303|PubMed:24361839};
GN Name=apbE2 {ECO:0000303|PubMed:24361839};
GN OrderedLocusNames=KPK_2905 {ECO:0000312|EMBL:ACI08719.1};
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, 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. Is responsible for the
CC modification of the fumarate reductase KPK_2907.
CC {ECO:0000250|UniProtKB:A5F5Y3, ECO:0000269|PubMed:24361839}.
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: Cytoplasm {ECO:0000269|PubMed:24361839}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene results in a complete
CC loss of the fumarate reductase activity displayed by KPK_2907, which
CC contains a covalently bound FMN, but does not affect the Na(+)-NQR
CC activity. {ECO:0000269|PubMed:24361839}.
CC -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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DR EMBL; CP000964; ACI08719.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XRA9; -.
DR SMR; B5XRA9; -.
DR EnsemblBacteria; ACI08719; ACI08719; KPK_2905.
DR KEGG; kpe:KPK_2905; -.
DR HOGENOM; CLU_044403_1_0_6; -.
DR OMA; SQVMDIN; -.
DR OrthoDB; 2021063at2; -.
DR BRENDA; 2.7.1.180; 2814.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..316
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000430777"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 88..90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
SQ SEQUENCE 316 AA; 35128 MW; FC057C28416A029F CRC64;
MSDNRVYSYS AVLMGSPILL KLYSHDEALA SRVFQLIKRY EDLLTVNRAE SQVMDINHAA
GRHPVTVSRP VFQLIQCAKA ASMVRDSAFN LAIGPLVKLW RIGFHGHSVP DAADIRARLA
LTRPQEVILD ETTCSVFLQQ PGMELDLGAI AKGYIADRVR DYLRQQQVEK ALINLGGNVH
TLGEWTIGLK KPFADAQALI GSLTINGQSV VTSGTYERYF EQDGKRWHHI LDPRSGYPLD
NELDSVTVIS TDSLDGDIWT TLLFGLGVEK GCAALRQRED IDAIFVTKNR DIILSSPQRL
RFSPLDSGYQ VIDCTA
