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
//