ID A0A0D0R3X2_9GAMM Unreviewed; 717 AA.
AC A0A0D0R3X2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:KIQ96399.1};
GN ORFNames=TI01_2077 {ECO:0000313|EMBL:KIQ96399.1};
OS Lysobacter sp. A03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ96399.1, ECO:0000313|Proteomes:UP000032077};
RN [1] {ECO:0000313|EMBL:KIQ96399.1, ECO:0000313|Proteomes:UP000032077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A03 {ECO:0000313|EMBL:KIQ96399.1,
RC ECO:0000313|Proteomes:UP000032077};
RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT "Genome sequence of Lysobacter sp. A03.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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:KIQ96399.1}.
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DR EMBL; JXSS01000095; KIQ96399.1; -; Genomic_DNA.
DR RefSeq; WP_043959201.1; NZ_JXSS01000095.1.
DR AlphaFoldDB; A0A0D0R3X2; -.
DR STRING; 1199154.TI01_2077; -.
DR PATRIC; fig|1199154.3.peg.862; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000032077; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000032077};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..190
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 244..561
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 583..690
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 717 AA; 77677 MW; DE6FEB1839216988 CRC64;
MDDRAFQRRW GWLALVLALA ALLWAWHAGL ADLLTLEQLK ARQADLSGWV GQNRWLAAGT
FFLVYVAVAA TSVPGAAVLT IAAGALFGLL EGTVLVSFAS SVGASLAFLV ARFALRDRLR
ARYREGLKKI DAGIAREGWR YLLTLRLVPV FPFFLVNLLA GLTALPLRTF YWVSQLGMLP
ATLVYVYAGT QLARIDSLAG VLSPGLLVAL VLLGALPLLA KGFTDWLAAR RVYRGHQKPR
AFDYNVLVIG AGSAGLVSAY IAATVKARVG LVEKDAMGGD CLNTGCVPSK ALLRTARLLA
ESRDSQRYGV RSMTAEFDFA DAMERVQEVI ARIAPHDSVE RYTGLGVEVI TGAARVVSPW
EIEVDGRRLS ARSLIIATGA RPLVPPIPGL DSVEYLTSDT LWGLRQLPGR LLVLGGGPIG
CELAQAFARF GSQVTVVEMA PRLLGREDAD AADAVARQLQ REGVHLATSH KALRVDGRGK
GGRLVCDHDG VEVTFEYDAL LLALGRSANV EGFGLEELGV RLNEGKTIEA DPMLRTNFPN
ILVCGDVTGP YQFTHVASHQ AWYATVNALL APWWSFTVDY RVIPWATFTD PEVARVGLSE
DEARQQEIAV EVTRYALDGL DRAITDGTDA GFVKVLTAPG KDRILGATIV GAHASEMLAE
FVLAMKHGIG LNKLLGTIHV YPTMTEANKH VAGNWKRANA PAGVLHWAKR YFAWRRG
//
