ID E6SE76_INTC7 Unreviewed; 469 AA.
AC E6SE76;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADU48724.1};
GN OrderedLocusNames=Intca_2215 {ECO:0000313|EMBL:ADU48724.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU48724.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU48724.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002343; ADU48724.1; -; Genomic_DNA.
DR RefSeq; WP_013493039.1; NC_014830.1.
DR AlphaFoldDB; E6SE76; -.
DR STRING; 710696.Intca_2215; -.
DR KEGG; ica:Intca_2215; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_1_11; -.
DR OMA; CIMASFD; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000008914; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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:UP000008914}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 48696 MW; B7F60C8EB5482965 CRC64;
MTTFPPSVQS RVVTDEDVKR TYAADAGPAP REPSRDVPSD YTVVRARDVA DVVAVLEHAQ
ATGTPVVPQG ARTSRVGGAR ATEGCIVLNV EALDAIETVD PVEGIAVVGP GVVNADLKTA
AAAAGLFYGP DPASTGTCTI GGNVATNAGG LCCLKYGVTA DWVTALDVVL PGGEVMRTGH
RTAKGVTGLD LTGLLVGSEG TLGVVTRVVT RLLPAPDPAL TALATFGSLD DAVRAVVTLR
LDRHRPSLLE ILDRASLEAV QAFGDYGFPA DADAVLLVQS DRPGHAAEDV ARYGELMTGA
GALEVAVAED RQEADLLLQG RRVLSTAIEA LGSRLAEDVC VPVGRLGDYV RGAAEVSERL
GVRIPVSGHA GDGNLHPSIV YPPGDDDARR RAWGAFDELM RLGLSLGGTV AGEHGIGSVK
RRWFAAEVGP REVQRQRAIK AVFDPSGIMN PEVVFGGGRW ATRPGSTST
//