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Database: UniProt
Entry: D2B2J1_STRRD
LinkDB: D2B2J1_STRRD
Original site: D2B2J1_STRRD 
ID   D2B2J1_STRRD            Unreviewed;       438 AA.
AC   D2B2J1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Cyclic nucleotide-regulated FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACZ91217.1};
GN   OrderedLocusNames=Sros_8575 {ECO:0000313|EMBL:ACZ91217.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ91217.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ91217.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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DR   EMBL; CP001814; ACZ91217.1; -; Genomic_DNA.
DR   RefSeq; WP_012894946.1; NC_013595.1.
DR   AlphaFoldDB; D2B2J1; -.
DR   STRING; 479432.Sros_8575; -.
DR   KEGG; sro:Sros_8575; -.
DR   eggNOG; COG1252; Bacteria.
DR   HOGENOM; CLU_021377_7_1_11; -.
DR   Proteomes; UP000002029; Chromosome.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF45; NADH DEHYDROGENASE-LIKE PROTEIN RV1812C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   DOMAIN          7..334
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   438 AA;  48093 MW;  4CEBE714A69F7B72 CRC64;
     MNRNSKHIVV VGGGYVGLYT VLRLQHTLRK ELREGSVRIT VLTPESHMTY QPFLPEAAAG
     NLSPRHVVVP LRRVLKRATI LNGKVSKVNH ATKTVAFEPN VGTPHEIGYD IVVMAAGSIS
     RTLPIPGLAD AAIGFKTIGE SIALRNRVLE LLDRAESDDD AGLRRRALTF VVIGGGFAGV
     EALAELEDMA VDAVRYYRNI SREDMRWVLV EATDRILPEV GPEMGKWTAE QLRERGIEVK
     MNTRLDSCEG GLVKLSDGEE FESATIVWTA GVKPSPVVNA GDLPLDERGR IKTTTRLTVA
     GVDDAFSAGD VAGVPDVTNP GQYCAPNAQH AVRQAKVLAD NITHLLHGEE LVDYRHKYVG
     SVAGLGLHKG VANVYGVKLR GLPAWFMHRT YHLSRVPTLN RKVRVMADWT LALFFKRETV
     SLGEIEAPRT EFRKAATY
//
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