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Database: UniProt
Entry: A0A0S8BIN4_9CHLR
LinkDB: A0A0S8BIN4_9CHLR
Original site: A0A0S8BIN4_9CHLR 
ID   A0A0S8BIN4_9CHLR        Unreviewed;       480 AA.
AC   A0A0S8BIN4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KPK11416.1};
GN   ORFNames=AMJ56_06220 {ECO:0000313|EMBL:KPK11416.1};
OS   Anaerolineae bacterium SG8_19.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK11416.1, ECO:0000313|Proteomes:UP000050892};
RN   [1] {ECO:0000313|EMBL:KPK11416.1, ECO:0000313|Proteomes:UP000050892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_19 {ECO:0000313|EMBL:KPK11416.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KPK11416.1}.
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DR   EMBL; LJNN01000058; KPK11416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8BIN4; -.
DR   PATRIC; fig|1703386.3.peg.3314; -.
DR   Proteomes; UP000050892; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        176..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..200
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   480 AA;  54460 MW;  B0237F106189BB95 CRC64;
     MNQLVQNDQT NFSLPLSRLE RVSAWGRASN AMSFVYRPST LEEIRRVLSI ANTSHRSIGL
     RGAGYSYGDA TLNGENITLD MRRMNRILDW NPEAGQIRVE PGVTISQLWQ YVLEDGWWPA
     VVPGTAKPTI GGCAGMNVHG KNAWKAGTIG DHIYEFELLL PSGDVVTCNR EDNRDLFFAT
     IGGFGMLGIF TSITLKLKRV YSGLLAVEAL ASSNIGEMID QFEDNLPNSD YLVGWIDAFA
     KGKSLGRGQI HLARYLPTGV DPSPHQTMRL DYQHLPDVMF GIMPRSIMWR FMRPLFNNLG
     ARFTNMGKYW SSKITHGSIF LQSHVAFHFL LDYVPNFKLA YGPGGLIQYQ CFVPKENALD
     AFSDLLRLCQ KRGLQNYLTV LKRHRPDEFL ISHGVDGYSM AMDFRVTPKR RSKLLALARE
     MDEIVINAAG RFYLAKDSTL RPETFHSYLG NNVIEQFRSL KEQHDPDSIL QTNMWRRLFD
//
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