APBE_HAEIN
ID APBE_HAEIN Reviewed; 346 AA.
AC P44550;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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:0000250|UniProtKB:A5F5Y3};
DE Flags: Precursor;
GN Name=apbE; OrderedLocusNames=HI_0172;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- 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 -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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DR EMBL; L42023; AAC21842.1; -; Genomic_DNA.
DR PIR; C64144; C64144.
DR RefSeq; NP_438340.1; NC_000907.1.
DR RefSeq; WP_005668096.1; NC_000907.1.
DR AlphaFoldDB; P44550; -.
DR SMR; P44550; -.
DR STRING; 71421.HI_0172; -.
DR EnsemblBacteria; AAC21842; AAC21842; HI_0172.
DR KEGG; hin:HI_0172; -.
DR PATRIC; fig|71421.8.peg.176; -.
DR eggNOG; COG1477; Bacteria.
DR HOGENOM; CLU_044403_0_0_6; -.
DR OMA; MGTYYSI; -.
DR PhylomeDB; P44550; -.
DR BioCyc; HINF71421:G1GJ1-182-MON; -.
DR Proteomes; UP000000579; 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; IBA:GO_Central.
DR GO; GO:0017013; P:protein flavinylation; IBA:GO_Central.
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; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..346
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000001749"
FT BINDING 34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 115..117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 299
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 346 AA; 37780 MW; 6A9D0E5DF5877B61 CRC64;
MKKLISGIIA VAMALSLAAC QKETKVISLS GKTMGTTYHV KYLDDGSITA TSEKTHEEIE
AILKDVNAKM STYKKDSELS RFNQNTQVNT PIEISADFAK VLAEAIRLNK VTEGALDVTV
GPVVNLWGFG PEKRPEKQPT PEQLAERQAW VGIDKITLDT NKEKATLSKA LPQVYVDLSS
IAKGFGVDQV AEKLEQLNAQ NYMVEIGGEI RAKGKNIEGK PWQIAIEKPT TTGERAVEAV
IGLNNMGMAS SGDYRIYFEE NGKRFAHEID PKTGYPIQHH LASITVLAPT SMTADGLSTG
LFVLGEDKAL EVAEKNNLAV YLIIRTDNGF VTKSSSAFKK LTETKE
