ID A0LQW5_ACIC1 Unreviewed; 453 AA.
AC A0LQW5;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ABK51825.1};
GN OrderedLocusNames=Acel_0049 {ECO:0000313|EMBL:ABK51825.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK51825.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK51825.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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}.
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DR EMBL; CP000481; ABK51825.1; -; Genomic_DNA.
DR RefSeq; WP_011718889.1; NC_008578.1.
DR AlphaFoldDB; A0LQW5; -.
DR STRING; 351607.Acel_0049; -.
DR KEGG; ace:Acel_0049; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_19_1_11; -.
DR InParanoid; A0LQW5; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06198; FNR_like_3; 1.
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; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-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; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..327
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 453 AA; 50207 MW; 213158F4EF865FD9 CRC64;
MTTNAIPARR ATSGVSLIRV RPGAVLTAIY LGGLAVLALW WHDTPPIHGW GEWLTNAGRI
TGLLAGYVVI VVLALMARVP AVERGVGADR LARWHAMGGR YLVGVAAAHT ALIIWGYAVS
AHEGLIRQTS DLLLHYPDVL MATVALGLFV GIGIVSARAL RRRLAYETWY YLHFYTYLAI
ALSFSHEFAT GADFMSNLPA RVLWAGLYIV VGAMLVWYRF LTPFRLALRH RFRVVRVVDE
APGIFSLHIG GRRLDELAIE PGQFFRWRFL CAGQWWQSHP YSLSAPPTRS LLRITVKALG
DHSTALRRIP PGTRVLAEGP YGALTAARRT SPRVLLIAGG IGITPLRALF ETLPGRRGDL
TLIYRANHEQ EFAFRAELDQ IARYRKAAVH YLVGPPGGPG DPFVGTRLRS LVPDVRRRDV
FVCGPPPMIT AAVTALRRLG VPRRRIHTEA FEF
//
