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Database: UniProt
Entry: D2B7E3_STRRD
LinkDB: D2B7E3_STRRD
Original site: D2B7E3_STRRD 
ID   D2B7E3_STRRD            Unreviewed;       402 AA.
AC   D2B7E3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ACZ91464.1};
GN   OrderedLocusNames=Sros_8831 {ECO:0000313|EMBL:ACZ91464.1};
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:ACZ91464.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ91464.1, 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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001814; ACZ91464.1; -; Genomic_DNA.
DR   RefSeq; WP_012895191.1; NC_013595.1.
DR   AlphaFoldDB; D2B7E3; -.
DR   STRING; 479432.Sros_8831; -.
DR   KEGG; sro:Sros_8831; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_2_1_11; -.
DR   Proteomes; UP000002029; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   DOMAIN          4..368
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          281..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  44411 MW;  DA130F95436E964C CRC64;
     MKSVIVVGAG IWGTSLALRL AESGWRVTLV EQYQPGHLRQ ASAGETRLLR ASHGTDDWYA
     RMARRARELW RDLGERVGEE LYAETGMLWF ARRAQGWERA SASVLERLDI PHEIWDPARA
     AALFPDFRGD DLEFVLWEPQ AGVVRARRAT QVTARLARAA GVTLVRGRAE PYGAGVLEPY
     DVVVPRGTEA YGMAFQGWAE PSGGPAVRVG DEVLRADRVV WACGAWLPRL FPGMADLQVT
     KQDTAHFAVA PGWDTPAWVD YDASVYGHGD LDGLGMKVTS DIEGEPYDPE TGDRRISPSS
     EEASRAYLRR RFPSLAQAPV LFSQVCQYTL TLDGEWVIAQ PEDGVWLLGG DSGHGFKHAP
     ALAEYVAEIL DGAREPEPRF GLHPRVPVRG LRTSGRTDRA DR
//
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