ID A0A1I6MF54_9BACT Unreviewed; 511 AA.
AC A0A1I6MF54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|ARBA:ARBA00016337};
DE EC=2.7.1.180 {ECO:0000256|ARBA:ARBA00011955};
DE AltName: Full=Flavin transferase {ECO:0000256|ARBA:ARBA00031306};
GN ORFNames=SAMN05421771_2512 {ECO:0000313|EMBL:SFS14340.1};
OS Granulicella pectinivorans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474950 {ECO:0000313|EMBL:SFS14340.1, ECO:0000313|Proteomes:UP000199024};
RN [1] {ECO:0000313|EMBL:SFS14340.1, ECO:0000313|Proteomes:UP000199024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21001 {ECO:0000313|EMBL:SFS14340.1,
RC ECO:0000313|Proteomes:UP000199024};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001219};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; FOZL01000001; SFS14340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6MF54; -.
DR STRING; 474950.SAMN05421771_2512; -.
DR OrthoDB; 195316at2; -.
DR Proteomes; UP000199024; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.4070; -; 1.
DR Gene3D; 3.10.520.10; ApbE-like domains; 1.
DR InterPro; IPR024932; ApbE.
DR InterPro; IPR003374; ApbE-like_sf.
DR InterPro; IPR014469; DUF2271.
DR PANTHER; PTHR30040:SF2; FAD:PROTEIN FMN TRANSFERASE; 1.
DR PANTHER; PTHR30040; THIAMINE BIOSYNTHESIS LIPOPROTEIN APBE; 1.
DR Pfam; PF02424; ApbE; 1.
DR Pfam; PF10029; DUF2271; 1.
DR SUPFAM; SSF143631; ApbE-like; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lipoprotein {ECO:0000313|EMBL:SFS14340.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199024};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..511
FT /note="FAD:protein FMN transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011796951"
SQ SEQUENCE 511 AA; 55335 MW; 542AFD9D19C59F3C CRC64;
MRKVFWSLAL AAVSAQGMAP FGVAAQSPRN TTAEDENTGV RVFHHENVLG TSLGLKLKTS
DAASAVRAES AVLVEIERCN RILSAWSPDS EFSHWLATRG TAEKVSSELI EVLSLFDAWR
TQTDGALDAS AETATKLWKN AALEQRPPTT RERETAVRTM QAEHWRIDRA AGTAVHLDDA
PIALNSFVKS YIAGRAADAA LASGATGVLL NLGGDLVARG ALTERVAIAD PAADAENDTP
LDLLHIQNRA VATSGGYRRG VTIDGQHISH LFDPRTAEPA LHVASATVIA QDAVEAGALA
TAFAVMQPAE TAALAARMRH VDYMLVLPDG SRVASPGWSL QQAPHIVRAA YISRATAPAQ
LDLLITLELA RISDPRYRRP YVSVWVEDKD HFPVKTIALW FEKARWLPDL KSWYHDDQIR
ALAEGTDLST TISSATRPPG KYTLRWDGKD NAGKPVKPGH YTICIEAARE HGSYQIIRQE
IDFDGRTARQ VTLPGGTEIG GVTLDYGAHA K
//
