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Database: UniProt
Entry: A0A1T2L5W5_9GAMM
LinkDB: A0A1T2L5W5_9GAMM
Original site: A0A1T2L5W5_9GAMM 
ID   A0A1T2L5W5_9GAMM        Unreviewed;       336 AA.
AC   A0A1T2L5W5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:OOZ40471.1};
GN   ORFNames=BOW52_05820 {ECO:0000313|EMBL:OOZ40471.1};
OS   Solemya elarraichensis gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918949 {ECO:0000313|EMBL:OOZ40471.1, ECO:0000313|Proteomes:UP000190198};
RN   [1] {ECO:0000313|EMBL:OOZ40471.1, ECO:0000313|Proteomes:UP000190198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp-SM6 {ECO:0000313|EMBL:OOZ40471.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OOZ40471.1}.
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DR   EMBL; MPRK01000088; OOZ40471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2L5W5; -.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000190198; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06189; flavin_oxioreductase; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT   DOMAIN          4..91
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          98..198
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   336 AA;  37203 MW;  C25C229B82D9414A CRC64;
     MSDFQVTIES NGQQFKVRKG EAILDAALHQ NVILPYGCRS GSCGSCAATL VEGEVEYPFG
     IPGGMPDEEG VCLTCQAQPL SDVTIRAEVL ETVEEIEVKA LPCKLEHMEQ LCHDVMGLYL
     KLPESQRLRF LAGQYLDIIL PNGHRRAFSI ANAPHDDEQI ELHVRYVAGG EFTETVFNLL
     QEKAVLRIEA PLGSFILREH SDRPMLFVAG GTGFAPIKAM IEHALYVGEK RPMKLYWGVR
     ASRDLYLPDL PQQWADENSN VDFVPVMSEP DGAWQGHSGF VHEAVIAEID DIADYDVYIA
     GPPVMVEACA AAFAEKGLSR DHMYSDVFEY AAAKEK
//
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