ID Q8KAS7_CHLTE Unreviewed; 452 AA.
AC Q8KAS7;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=NADH oxidase, putative {ECO:0000313|EMBL:AAM73295.1};
GN OrderedLocusNames=CT2078 {ECO:0000313|EMBL:AAM73295.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM73295.1, ECO:0000313|Proteomes:UP000001007};
RN [1] {ECO:0000313|EMBL:AAM73295.1, ECO:0000313|Proteomes:UP000001007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000313|Proteomes:UP000001007};
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA Deboy R., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.L., Yang F., Holt I., Umayam L.A., Mason T.,
RA Brenner M., Shea T.P., Parksey D., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J., Khouri H., White O.,
RA Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; AE006470; AAM73295.1; -; Genomic_DNA.
DR RefSeq; NP_662953.1; NC_002932.3.
DR RefSeq; WP_010933733.1; NC_002932.3.
DR AlphaFoldDB; Q8KAS7; -.
DR SMR; Q8KAS7; -.
DR STRING; 194439.CT2078; -.
DR EnsemblBacteria; AAM73295; AAM73295; CT2078.
DR KEGG; cte:CT2078; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_10; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001007}.
FT DOMAIN 6..303
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 452 AA; 48160 MW; E2D7890879425717 CRC64;
MNKQVDVLVI GGSAAGIVAA TTGKAFYASK SFLIVRKEPE AVVPCGIPYI FGTLDGVHQN
IVPTAPLANA DVELLIDEVV SIDREAKSAT TAGGVVISWD KLVLATGSEP KTPDWLEGRD
LDGVFVIPKN RDYLCRLRSR LEEPRRVAII GGGFIGVELA DELAKKGHDV TLVEILPHVL
SMAFDSDLSL KAEELLVKRG VKLKTGEKLK KLAGQASVSK VILESGEEIE VDIVILATGY
APNVELARSA GIKINELGAI RVDEYMRTED KNIFAVGDCA EKFSFITRIV KGLMLASTAC
SEARIAGMNL FGLSRLRTFS GTIAIFSTAI GGTTFAAAGV TEQLARERGF EVVSAGFTGI
DKHPGTLPET SNQYVKLIVN SENGLVLGGA VMGGQSAGEL INVIGVIIET KMTVNELLTL
QFGTHPLLTG PPTAYALIKA AEAVEMKLRH FK
//
