ID A0A401Y614_9ACTN Unreviewed; 468 AA.
AC A0A401Y614;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:GCD90036.1};
GN ORFNames=NLS1_20420 {ECO:0000313|EMBL:GCD90036.1};
OS Nocardioides sp. LS1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1027620 {ECO:0000313|EMBL:GCD90036.1, ECO:0000313|Proteomes:UP000288271};
RN [1] {ECO:0000313|EMBL:GCD90036.1, ECO:0000313|Proteomes:UP000288271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS1 {ECO:0000313|EMBL:GCD90036.1,
RC ECO:0000313|Proteomes:UP000288271};
RA Morimura H., Sato I., Uesaka K.;
RT "Draft Genome sequence of the deoxynivalenol-degrading actinomycete
RT Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:GCD90036.1}.
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; BIFF01000002; GCD90036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Y614; -.
DR Proteomes; UP000288271; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000288271};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 237..337
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 468 AA; 50883 MW; 371E9A463A8EA168 CRC64;
MTTVTPPRAS RRLDAPAPLG RRARADAVVR QASGSLLWLG LLLVTYWWAA GGGIQDLGAW
ASGLTSVGRL TGLVASVLLL AQVALMARVP RLESAFGQDR LAHLHRIVGF TSFNLMLAHV
VTITWGYAGG QLPGTPGTLW NLTVNYPGML LAVAGTACLV MVVVTSLRAA RRRLRYESWH
LLHLYAYLGV GLALPHQLWT GHELTSSTAR TVFWWAAWGA VAGAVLIWRV GVPLAVNLRH
QLRVTSVVPE GHGIVSVYLT GRRLDLLRAE AGQFFTWRFL GRSGWSRANP YSLSAAPDGR
SLRITIQAVG DGSAEALRLH PGTRVLVEGP YGRLSARSRS RGKVALIGAG VGVTPLRALA
EGLDYAPGDA VLLQRYGDDR LFARELDVLT HERGLRVVPL PGHRRGRDSW LGEVGHGSDL
DHLHRWVPDI AERDVYVCGP TPWADLVVED LTSAGVTPDH IHLETFAW
//
