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Database: UniProt
Entry: A0A1S1QLI6_9ACTN
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ID   A0A1S1QLI6_9ACTN        Unreviewed;       965 AA.
AC   A0A1S1QLI6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OHV33164.1};
GN   ORFNames=CC117_23605 {ECO:0000313|EMBL:OHV33164.1};
OS   Parafrankia colletiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV33164.1, ECO:0000313|Proteomes:UP000179627};
RN   [1] {ECO:0000313|Proteomes:UP000179627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA   Hurst S.;
RT   "Sequence Frankia sp. strain CcI1.17.";
RL   Submitted (JUL-2016) 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:OHV33164.1}.
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DR   EMBL; MBLM01000134; OHV33164.1; -; Genomic_DNA.
DR   RefSeq; WP_071087333.1; NZ_MBLM01000134.1.
DR   AlphaFoldDB; A0A1S1QLI6; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000179627; 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; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179627}.
FT   DOMAIN          38..260
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          592..622
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   965 AA;  101785 MW;  F2191A037FD7769B CRC64;
     MTDSDERAGV SAALRAAGLE VRDDPGTRAM YATDASLYRI PPLAVVRPRH VDDVACALDV
     ARAFGVGITA RGAGTSIAGN AIGRGIVLDF SRHLGRVLEI DAGTRTAVVE PGTVHAVLQR
     AALPLGLRFG PDPSSHSRCT VGGMIGNNAC GNRALGYGRT SDNVVAMTHL LASGETLRTG
     YDAAGAPVVD GPARLLADLR AAAGRHLATA RTEFDTFGRQ LSGYAVAHLL PERFDLGRAL
     VGSEGTLGLL TQATVRLVKD PEHRVVVAIG FADIVQAGEA APAVVAFGPT ACEGMDQRLV
     DVLRGRRGDT AVPPLPRGAA WLFVEVAGDD HAEVLDRAGA LAAAGLGTQA RIVTDPAEQA
     RLWRIREDGA GLAGRAPSGR PAWPGLEDAA VPPQRLGAYL ARFDELVAAH GMTCAPYGHF
     GDGCMHVRLD FPFDRPDGLR VLREFLTAAA GLVAEFGGSI SGEHGDGRAR GELLARMYSA
     DAIRLFGEVK HAFDPDNRLN PGVLTAPDPF DADVRMVGVT YRRDLAFAYP HDGGDLAEAV
     HRCTGVGRCR ADTRTGGGVM CPSYLATREE KDSTRGRARV LQDVVRGDLD WRAPDVHDAL
     DLCLACKGCA SDCPTGIDMA MYKAEALHQK YRRRGWRRPG YRLGLRPRSH YTLGWLPRWA
     RLAGRAPRLA NALPTLPVLG RLGLYLAGVD RRRTVPAFAP TPFRRWWAAQ LVGGPEVADG
     SGGGTPVMLF VDTFSDHFTP SAARAVVRVL RAAGYQPRIP SAGACCGLTW ITTGQLDTAR
     RILGRTVTEL AASARAGIPI VGIEPSCTAV LRADAVELLG RTDHAEDARL VAAATRTVAE
     LLTATPAWAP PDLTGTAVIA QPHCHHHAVL GWAADRALLE RAGAQVTTLD GCCGLAGNFG
     VEIGHHEVSV AVAGQHLLPG LDAAPGAVVL ADGFSCRTQI TDLRGRRALH LAELLSPDPG
     PSPGA
//
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