ID C6WM63_ACTMD Unreviewed; 495 AA.
AC C6WM63;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACU34797.1};
GN OrderedLocusNames=Amir_0836 {ECO:0000313|EMBL:ACU34797.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34797.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU34797.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001630; ACU34797.1; -; Genomic_DNA.
DR AlphaFoldDB; C6WM63; -.
DR STRING; 446462.Amir_0836; -.
DR KEGG; ami:Amir_0836; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_4_4_11; -.
DR Proteomes; UP000002213; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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; IPR041575; Rubredoxin_C.
DR PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT DOMAIN 3..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..375
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 424..467
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 495 AA; 50733 MW; 26C97868CF386156 CRC64;
MRRVVVVGHG MAGARFAEEV LRRDPGGERV GLTLLGAERH PAYNRVLLSS VVAGSLPPES
VRLHAPDWAE RSAADLRLGA SVGKVDRVRR VVQVDDGEVP YDALVLATGA RPWLPPVAGL
VGVDGVLAPG AVAFRTLDDC AAITSAARPG APVVVLGGGL LGLEAARGLV ARGCLVTVVH
PRSHLMERQL DAGAGRVLAR ALGGLGVELR LGAVAERYEP GEGLRLADGT RLAADLLVVA
AGVRPAVELA AQAGIAVDRG VLVDDALRTD DPRVHAIGDC AQHEGAPTGL VQPAWEQAAV
LADRLTGTDP AARYRGGGAV TRLKARDVDL VALGEVHVGV DDERAEVLAL EDPARGRYAK
LVLRDDRVTG AILLGVPDAA AAVTQLYDRG LPAPSDRLGL LLGRALPAGA VAEASPADLP
AGAVVCRCNT VSKGQLVSAW RAGARSAPGL VEATRAGTGC GGCRDAVCGI ADWLAAAEPS
TASAVENQRS AVRGL
//
