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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//