ID Q8KEW7_CHLTE Unreviewed; 494 AA.
AC Q8KEW7;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Oxidoreductase, FAD-binding {ECO:0000313|EMBL:AAM71807.1};
GN OrderedLocusNames=CT0565 {ECO:0000313|EMBL:AAM71807.1};
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:AAM71807.1, ECO:0000313|Proteomes:UP000001007};
RN [1] {ECO:0000313|EMBL:AAM71807.1, 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};
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DR EMBL; AE006470; AAM71807.1; -; Genomic_DNA.
DR RefSeq; NP_661465.1; NC_002932.3.
DR RefSeq; WP_010932252.1; NC_002932.3.
DR AlphaFoldDB; Q8KEW7; -.
DR STRING; 194439.CT0565; -.
DR EnsemblBacteria; AAM71807; AAM71807; CT0565.
DR KEGG; cte:CT0565; -.
DR PATRIC; fig|194439.7.peg.529; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_10; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001007}.
FT DOMAIN 21..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 494 AA; 54843 MW; 6BCD5BF41CBBEFF6 CRC64;
MNFKNEPAAI AGFLEDTSNL KNGWTPGVFF PETPEEVASL LREACADGRR YTIAGNGTGT
TGARIPFGDY VIAMQKLDRI GEVEPTIDGR ALLRVQGGAL LQDVQAKAAA AGWFYPPDPT
EKTCFIGSTI SNNSTGSRSL KYGPTRNHVQ ALQIALPQGD LLEITRGQHL ADAAGNFTLD
LPLAGRVTFR LPDYTMPKTS KHNAGYWSKP GMDLVDLFIG SEGTLGVIVE ATLLLRPAPE
RVIACLAWFR SEEELLGFVG EARAGSGGVS PRALELFDRR ALEFLRQSYP DIAKEMAGAV
YFEEETTVER EEACLEAWLE LMEQCGSPVE KSWAALDSEG LQKLRDFRHQ LPVLVNEWLS
RQSESKVSTD MALPDERFAE LFRLYRDACD REGFTYIIFG HIGNAHLHLN ILPHNHEEFV
RAKTLYRQLV SKVLAMGGTL SAEHGIGKLK SEYLVQMYGR KGIREMVRVK KAFDPYLVLN
VGNMIPAEYY ESET
//
