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FAD:protein FMN transferase (EC 2.7.1.180) (Flavin transferase)

 APBE_TREPA              Reviewed;         362 AA.
O83774;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 97.
RecName: Full=FAD:protein FMN transferase {ECO:0000250|UniProtKB:A5F5Y3};
EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3};
AltName: Full=Flavin transferase {ECO:0000250|UniProtKB:A5F5Y3};
Flags: Precursor;
Name=apbE; OrderedLocusNames=TP_0796;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=9665876; DOI=10.1126/science.281.5375.375;
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
Weidman J.F., Smith H.O., Venter J.C.;
"Complete genome sequence of Treponema pallidum, the syphilis
spirochete.";
Science 281:375-388(1998).
[2]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 23-362 IN COMPLEXES WITH
ADP; AMP; FAD AND MAGNESIUM, FUNCTION, COFACTOR, AND SUBUNIT.
PubMed=23447540; DOI=10.1074/jbc.M113.449975;
Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V.;
"The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent
FAD pyrophosphatase with a potential role in flavin homeostasis.";
J. Biol. Chem. 288:11106-11121(2013).
-!- FUNCTION: 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 (By similarity).
Displays FAD pyrophosphatase activity in vitro, hydrolyzing FAD
into FMN and AMP (PubMed:23447540). {ECO:0000250|UniProtKB:A5F5Y3,
ECO:0000269|PubMed:23447540}.
-!- CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L-
threonine + AMP. {ECO:0000250|UniProtKB:A5F5Y3}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:23447540};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:23447540};
Note=Magnesium. Can also use manganese.
{ECO:0000269|PubMed:23447540};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23447540}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-
ProRule:PRU00303}; Lipid-anchor {ECO:0000250|UniProtKB:P41780,
ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side
{ECO:0000250|UniProtKB:P41780}.
-!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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EMBL; AE000520; AAC65759.1; -; Genomic_DNA.
PIR; C71281; C71281.
PDB; 4IFU; X-ray; 1.83 A; A=23-362.
PDB; 4IFW; X-ray; 2.30 A; A=23-362.
PDB; 4IFX; X-ray; 1.45 A; A=23-362.
PDB; 4IFZ; X-ray; 1.90 A; A=23-362.
PDB; 4IG1; X-ray; 1.43 A; A=23-362.
PDB; 4XDR; X-ray; 1.40 A; A=23-362.
PDB; 4XDT; X-ray; 1.45 A; A=23-362.
PDB; 4XDU; X-ray; 1.35 A; A=23-362.
PDBsum; 4IFU; -.
PDBsum; 4IFW; -.
PDBsum; 4IFX; -.
PDBsum; 4IFZ; -.
PDBsum; 4IG1; -.
PDBsum; 4XDR; -.
PDBsum; 4XDT; -.
PDBsum; 4XDU; -.
ProteinModelPortal; O83774; -.
SMR; O83774; -.
STRING; 243276.TP0796; -.
EnsemblBacteria; AAC65759; AAC65759; TP_0796.
KEGG; tpa:TP_0796; -.
eggNOG; ENOG4105CJ2; Bacteria.
eggNOG; COG1477; LUCA.
KO; K03734; -.
OMA; MGTFWRV; -.
Proteomes; UP000000811; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0017013; P:protein flavinylation; IEA:InterPro.
InterPro; IPR024932; ApbE.
InterPro; IPR003374; ApbE-like_sf.
PANTHER; PTHR30040; PTHR30040; 1.
Pfam; PF02424; ApbE; 1.
PIRSF; PIRSF006268; ApbE; 1.
SUPFAM; SSF143631; SSF143631; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
FAD; Flavoprotein; Lipoprotein; Magnesium; Membrane; Metal-binding;
Palmitate; Reference proteome; Signal; Transferase.
SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 23 362 FAD:protein FMN transferase.
/FTId=PRO_0000001751.
NP_BIND 118 120 FAD. {ECO:0000269|PubMed:23447540}.
NP_BIND 278 280 FAD. {ECO:0000269|PubMed:23447540}.
METAL 184 184 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:23447540}.
METAL 306 306 Magnesium. {ECO:0000269|PubMed:23447540}.
METAL 310 310 Magnesium. {ECO:0000269|PubMed:23447540}.
BINDING 181 181 FAD. {ECO:0000269|PubMed:23447540}.
BINDING 187 187 FAD. {ECO:0000269|PubMed:23447540}.
LIPID 23 23 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
LIPID 23 23 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
STRAND 30 38 {ECO:0000244|PDB:4XDU}.
STRAND 41 49 {ECO:0000244|PDB:4XDU}.
HELIX 53 74 {ECO:0000244|PDB:4XDU}.
STRAND 79 81 {ECO:0000244|PDB:4XDR}.
HELIX 82 88 {ECO:0000244|PDB:4XDU}.
TURN 89 91 {ECO:0000244|PDB:4XDU}.
STRAND 95 97 {ECO:0000244|PDB:4XDU}.
HELIX 99 114 {ECO:0000244|PDB:4XDU}.
TURN 115 117 {ECO:0000244|PDB:4XDU}.
HELIX 124 136 {ECO:0000244|PDB:4XDU}.
HELIX 142 149 {ECO:0000244|PDB:4XDU}.
HELIX 154 156 {ECO:0000244|PDB:4XDU}.
STRAND 157 161 {ECO:0000244|PDB:4XDU}.
STRAND 169 173 {ECO:0000244|PDB:4XDU}.
TURN 183 185 {ECO:0000244|PDB:4XDU}.
HELIX 186 200 {ECO:0000244|PDB:4XDU}.
STRAND 206 210 {ECO:0000244|PDB:4XDU}.
STRAND 213 218 {ECO:0000244|PDB:4XDU}.
STRAND 234 239 {ECO:0000244|PDB:4XDU}.
STRAND 245 263 {ECO:0000244|PDB:4XDU}.
STRAND 266 271 {ECO:0000244|PDB:4XDU}.
STRAND 274 278 {ECO:0000244|PDB:4XDU}.
TURN 282 284 {ECO:0000244|PDB:4XDU}.
STRAND 285 287 {ECO:0000244|PDB:4XDU}.
STRAND 293 300 {ECO:0000244|PDB:4XDU}.
HELIX 302 315 {ECO:0000244|PDB:4XDU}.
HELIX 317 324 {ECO:0000244|PDB:4XDU}.
STRAND 331 335 {ECO:0000244|PDB:4XDU}.
STRAND 339 343 {ECO:0000244|PDB:4XDU}.
TURN 345 347 {ECO:0000244|PDB:4XDU}.
HELIX 348 350 {ECO:0000244|PDB:4XDU}.
STRAND 351 355 {ECO:0000244|PDB:4XDU}.
STRAND 358 360 {ECO:0000244|PDB:4XDU}.
SEQUENCE 362 AA; 39064 MW; E64E2FAFD1A7041C CRC64;
MKSSCVYWRI GVLVCILCGV GSCGGRARVR EYSRAELVIG TLCRVRVYSK RPAAEVHAAL
EEVFTLLQQQ EMVLSANRDD SALAALNAQA GSAPVVVDRS LYALLERALF FAEKSGGAFN
PALGAXVKLW NIGFDRAAVP DPDALKEALT RCDFRQVHLR AGVSVGAPHT VQLAQAGMQL
DLGAIAKGFL ADKIVQLLTA HALDSALVDL GGNIFALGLK YGDVRSAAAQ RLEWNVGIRD
PHGTGQKPAL VVSVRDCSVV TSGAYERFFE RDGVRYHHII DPVTGFPAHT DVDSVSIFAP
RSTDADALAT ACFVLGYEKS CALLREFPGV DALFIFPDKR VRASAGIVDR VRVLDARFVL
ER


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