APBE_VIBC3
ID APBE_VIBC3 Reviewed; 334 AA.
AC A5F5Y3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=FAD:protein FMN transferase {ECO:0000303|PubMed:23558683};
DE EC=2.7.1.180 {ECO:0000269|PubMed:23558683};
DE AltName: Full=Flavin transferase {ECO:0000303|PubMed:23558683};
DE Flags: Precursor;
GN Name=apbE {ECO:0000303|PubMed:23558683};
GN OrderedLocusNames=VC0395_A1878 {ECO:0000312|EMBL:ABQ20132.1},
GN VC395_2405 {ECO:0000312|EMBL:ACP10395.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
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).
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. Cannot use directly FMN instead of FAD as
CC substrate. {ECO:0000269|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:0000269|PubMed:23558683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23558683};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ20132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACP10395.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ20132.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP10395.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001246830.1; NZ_JAACZH010000008.1.
DR PDB; 6NXI; X-ray; 1.61 A; A=18-334.
DR PDB; 6NXJ; X-ray; 1.92 A; A/B=18-334.
DR PDBsum; 6NXI; -.
DR PDBsum; 6NXJ; -.
DR AlphaFoldDB; A5F5Y3; -.
DR SMR; A5F5Y3; -.
DR STRING; 345073.VC395_2405; -.
DR EnsemblBacteria; ABQ20132; ABQ20132; VC0395_A1878.
DR GeneID; 57740910; -.
DR KEGG; vco:VC0395_A1878; -.
DR KEGG; vcr:VC395_2405; -.
DR PATRIC; fig|345073.21.peg.2318; -.
DR eggNOG; COG1477; Bacteria.
DR HOGENOM; CLU_044403_0_0_6; -.
DR BioCyc; MetaCyc:MON-18021; -.
DR BRENDA; 2.7.1.180; 15862.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000249; Chromosome 2.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Palmitate; Signal;
KW Transferase.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 17..334
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000430778"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 110..112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 259
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P41780"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 48..66
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:6NXI"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:6NXI"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:6NXJ"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6NXJ"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:6NXI"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6NXI"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6NXI"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6NXI"
SQ SEQUENCE 334 AA; 36784 MW; 32D7CCB1160CD8EA CRC64;
MRNWLVALAS LLLLAGCEKP AEQVHLSGPT MGTTYNIKYI QQPGIADSKT LQTEIDRLLE
EVNDQMSTYR KDSELSRFNQ HTSSEPFAVS TQTLTVVKEA IRLNGLTEGA LDVTVGPLVN
LWGFGPEARP DVVPTDEELN ARRAITGIEH LTIEGNTLSK DIPELYVDLS TIAKGWGVDV
VADYLQSQGI ENYMVEIGGE IRLKGLNRDG VPWRIAIEKP SVDQRSVQEI IEPGDYAIAT
SGDYRNYFEQ DGVRYSHIID PTTGRPINNR VVSVTVLDKS CMTADGLATG LMVMGEERGM
AVAEANQIPV LMIVKTDDGF KEYASSSFKP FLSK
