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Database: UniProt
Entry: A0A0M8SLG8_9ACTN
LinkDB: A0A0M8SLG8_9ACTN
Original site: A0A0M8SLG8_9ACTN 
ID   A0A0M8SLG8_9ACTN        Unreviewed;       993 AA.
AC   A0A0M8SLG8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KOU36189.1};
GN   ORFNames=ADK51_04780 {ECO:0000313|EMBL:KOU36189.1};
OS   Streptomyces sp. WM6368.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU36189.1, ECO:0000313|Proteomes:UP000037718};
RN   [1] {ECO:0000313|EMBL:KOU36189.1, ECO:0000313|Proteomes:UP000037718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6368 {ECO:0000313|EMBL:KOU36189.1,
RC   ECO:0000313|Proteomes:UP000037718};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOU36189.1}.
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DR   EMBL; LGDA01000013; KOU36189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8SLG8; -.
DR   PATRIC; fig|1415554.3.peg.990; -.
DR   Proteomes; UP000037718; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
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; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          81..309
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          577..608
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   993 AA;  106250 MW;  2577B39449A9D031 CRC64;
     MKRSARGRGR REGTPVPLLE PRPGALRPRS VDGPAPDKVP DHRAAGTPEP LRTELAELLG
     PQKVLWKVSD LVRYASDASP YRFVPQVVVV AEDIDDVSAV LSYAHGRQRE VVFRAAGTSL
     NGQAQGEDIL VDVRRHWAGI EVLEEGRRAR IRPGTTVARA NAALARHGRV LGPDPASAIA
     CTVGGVVANN ASGMTAGTTR NSYRTLSSLT FVLPGGTVVD TADPLADEEL ARAEPALCHG
     LMEIKREIEA DPALVARIRA KYEIKNTTGY RLDAYLDGTT PVEILRGLMV GSEGTLGFIC
     EVVFDTLPLE REVCTALLFF PSLPAAAAAV PLFNAAGAVA VELMDGNTLR ASVSVPGVPA
     DWADLPRETT ALLVEFRAPD PAGRDTCAQR AARVLDGLDL VAPVPSVTNT FTSDPRTVGG
     YWQARRAFVT AVGGARARGT TLITEDFAVP PSRLAEACEA LLALQAEHGF DAAVAGHAAH
     GNLHFMLAFD AADPADVERY GAFMEAFCRL TVERFDGSLK AEHSTGRNMA PFLELEWGPV
     ATGLMWRTKH LVDPEGVLAP RVLLDRDPRA HLRGLKTIPQ VEEVVDPCIE CGFCEPACPS
     GDLTTTPRQR IVLRREMLRQ QPGSAVLDGL LASYGYDAVD TCAADSTCRL ACPVGIDTGA
     LMKDFRHRRH GPREEAAAAL AARRFGAAES AARLAVSAAD RIPFRIGTGL LGAVTAAARR
     AVRPDLVPQW PARLPGPAAR HLPPTRRVGA AAVYYPACVN RIFGGPEGRP GPSLPEAVVA
     LSERAGRPVW IPGDLGGTCC ATIWHSKGYE AGARVMANRI VEAAWGWTAG GRLPLVVDAS
     SCTLGIAREV VAYLTRENRA LHAQLRVLDS IVWAAEELLP HLEVRRTVGS AVLHPTCSMR
     HLGDEDRLRA VAEACAEEVV VPEEAGCCAF AGDRGMLHPE LTASATAREA AEVTARPFDA
     HLSANRMCEV GMDRATGRRY YSALLELERA TRP
//
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