ID C7Q5W0_CATAD Unreviewed; 447 AA.
AC C7Q5W0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACU70057.1};
GN OrderedLocusNames=Caci_1131 {ECO:0000313|EMBL:ACU70057.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU70057.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU70057.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CP001700; ACU70057.1; -; Genomic_DNA.
DR RefSeq; WP_012785351.1; NC_013131.1.
DR AlphaFoldDB; C7Q5W0; -.
DR STRING; 479433.Caci_1131; -.
DR KEGG; cai:Caci_1131; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_0_11; -.
DR InParanoid; C7Q5W0; -.
DR OrthoDB; 5169292at2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 34..206
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 447 AA; 46192 MW; FFE9B7BD71F181F9 CRC64;
MTATTTLEIL SRDFSGDIIE PGHAEYAAAS GVVLAAGAPA VILRPSSVGG VQAAVRHAAA
SGLPLAVRGG GHSFGGFGTN DGGVVIDLSR LCGVEVVAGG WNVVRVGGGA TWGQVTAALK
PHRLALSSGD TKGVGVGGLT LGGGIGWKVR KYGLALDSLV RVEIVTADGH VVTADEDENA
DLFWAVRGGG GNFGIVTAFE FAGHPTTDVF HGKISFPGAE AATVIPAWAE YMRTAPEALT
TIAVFANPFA GPGAPVEILV TFDGDATDEA DAAIDPLRRL GTLIDDDITL KPYGDVLEEA
PPLPPALRFH TRNAFVERAG VDAALRIMTE AGAAPGAPFL TARSLGGALA RVPDDATAFA
HRRAELMIGT ALVGPEPVIE AAIPALDALW ERLTPHVNGT YPNFNTTATD QEIAAAYPTD
TYKRLAAVKR HYDPANLFTA NYNVLPL
//
