ID D1AA98_THECD Unreviewed; 411 AA.
AC D1AA98;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACY98811.1};
GN OrderedLocusNames=Tcur_3272 {ECO:0000313|EMBL:ACY98811.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98811.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY98811.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001738; ACY98811.1; -; Genomic_DNA.
DR RefSeq; WP_012853595.1; NC_013510.1.
DR AlphaFoldDB; D1AA98; -.
DR STRING; 471852.Tcur_3272; -.
DR KEGG; tcu:Tcur_3272; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_0_1_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001918; 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 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 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:UP000001918}.
FT DOMAIN 29..207
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 411 AA; 42363 MW; 375DB65AC18CEEB8 CRC64;
MDALHKRALS ALSRVCGEVR EGLPAEGVLG VVPAVVAAPR TVAEAAEVMR VAAELELAVV
PRGGETRLEW GLPPERCDLL IDTTGLARVV EHAAGDLVVT VEAGVTLGRL AEVLAGAGQR
LALDVPTPHS TVGGTVAAGA GGPSRLLHGS VRDLLIGVTM IRADGRIARS GGKVVKNVAG
YDLGRLLAGS FGTLGLIVEA AFRLHPLPGA RAYVSGEFGD VAQAHRAAQR VLHSPHVPSA
IEVDTEIGGA VRLCVLLEGV PEGVAARAEA VADLLGAGAR IADAPPPWWG LYPDGTTLIE
LTGPPTALPR IVGTLQEHRA AETVLRGSAG AGIWHVGLGS AEPQAVAKLL ADLRGMLAPL
PGGAVVRYAP QAVREEIDLW GPIPALALMR RVKEQFDPGR RLSPGRFAGG I
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