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Database: UniProt
Entry: A0A177QZ48_9PLAN
LinkDB: A0A177QZ48_9PLAN
Original site: A0A177QZ48_9PLAN 
ID   A0A177QZ48_9PLAN        Unreviewed;       883 AA.
AC   A0A177QZ48;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AYO47_06165 {ECO:0000313|EMBL:OAI52455.1};
OS   Planctomyces sp. SCGC AG-212-M04.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1799657 {ECO:0000313|EMBL:OAI52455.1, ECO:0000313|Proteomes:UP000186875};
RN   [1] {ECO:0000313|Proteomes:UP000186875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-M04 {ECO:0000313|Proteomes:UP000186875};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAI52455.1}.
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DR   EMBL; LSTH01000209; OAI52455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QZ48; -.
DR   Proteomes; UP000186875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.520.10; ApbE-like domains; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like_sf.
DR   InterPro; IPR007329; FMN-bd.
DR   PANTHER; PTHR30040:SF2; FAD:PROTEIN FMN TRANSFERASE; 1.
DR   PANTHER; PTHR30040; THIAMINE BIOSYNTHESIS LIPOPROTEIN APBE; 1.
DR   Pfam; PF02424; ApbE; 1.
DR   Pfam; PF12801; Fer4_5; 2.
DR   Pfam; PF04205; FMN_bind; 2.
DR   SMART; SM00900; FMN_bind; 2.
DR   SUPFAM; SSF143631; ApbE-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186875};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        352..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        378..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        501..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        550..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..186
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
FT   DOMAIN          246..334
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   883 AA;  95487 MW;  D2B05505B83271EF CRC64;
     MDDLLPVVDE PRAAFHPLPP PVRWLVRLTR AAILVVAFLL IARSDRAADE ANVIPFETAL
     QLFPTAARLG PRDARLNGWT VLASDGHPLG IVFETSPQTD HLVGYSGPSN LLLGLDPQGA
     IVGVRFLSSR DTTEHVEQVR SHPAFWSQFR GWNPTSDPRP RVDAVSGSTL TSYAMAESIE
     ERLAGHSTSL RFPNAISLEE ARGVFPEAQS LKPDSTRLGW LEVRGAEEQL LGFVLRTSPY
     AESVRGYSGP TEALIAVDPT RTRVAAIRMR SSYDTPDYAA RVRADEEYLR SLADHTLEEW
     TQIDFESAGI EGVSGSTQTS YGLAEGIRRR LKADLANVPA AVGGKLWKRR NFGLLAIIAG
     GLLVTFVPAF GGRRIRTLWQ IVLVAAFGLW LGDMLSMALL AGWARNGVAW STAPGLVALV
     AVALVVPWST KRQVYCHSLC PHGAVQEWLG HERRCHVHVP RRLSRLLGLL PGTLLAVAFG
     LSLTKPRFNL ARFEPFDAWV LWTAAAVSML VGLAGLVAAV FVPMAYCRFG CPTGALLKLV
     RSHGQADRWS LRDFIAAAAV SLAAAWMFWS APAKTVNASG SPTASVVLTG PSTLTGRAFG
     TTWTIKIRDP LASTGVLQEQ VAAELERIES KLSHWRPGSE TSQFNASQTT LEIECSKELA
     SLVSQARGLS EATDGAFDIT VGPLVNAWGY GPSGPKPDPP SVVKIRKLLD STGWQKLEVD
     ESVPSLRKQD PALQIDLGAL LQGYAVDRVH DLLAKHGLKE YLVEIGGELR ASGAWEVALD
     PAAGAWSTPT IKLRDQALST SGVYRRGPNG EEKHVISPRT GRPAATAWRA VAVMAPTCRE
     ADGWDTALLV AADGRALAEQ RGFKAQFIPR EGPAVQVGDW SAK
//
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