ID A0A157SSZ6_9BORD Unreviewed; 354 AA.
AC A0A157SSZ6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:SAI73465.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:SAI73465.1};
DE EC=1.17.1.- {ECO:0000313|EMBL:SAI73465.1};
GN Name=ascD_2 {ECO:0000313|EMBL:SAI73465.1};
GN ORFNames=SAMEA3906486_04646 {ECO:0000313|EMBL:SAI73465.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI73465.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI73465.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI73465.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FKIF01000009; SAI73465.1; -; Genomic_DNA.
DR RefSeq; WP_011516092.1; NZ_FKIF01000009.1.
DR AlphaFoldDB; A0A157SSZ6; -.
DR STRING; 288768.SAMEA3906486_04646; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000076848; 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:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd00207; fer2; 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};
KW Oxidoreductase {ECO:0000313|EMBL:SAI73465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076848}.
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 354 AA; 39206 MW; 4A71F38DC46564AA CRC64;
MTYQLNIQPL GATIEVEEGQ TILDAALRQG IYIPHACGHG LCGTCKVQVC DGEVDLGDAN
LFALMDFERE ERKALACCAT LLDDTTIEAD IEEDPDAEVI PVEDFNAEVT RIEQLTPTIK
AVFLRLDQPI HFQAGQYVQL EIPELRQTRA FSIANSPADV AATGEIELNI RRVPGGQGTG
YIHEQLAVGN ILHVTGPYGR FFVRRSADQP MVFMAGGSGL SSPRSMILDL LQSGWSKPIT
LVYGQRNEAE LYYDDEFREL SQRYSNFSYV PALSEKAEGA THPLAQGFVH EVAKAHFQNN
FSGHQAYLCG PPAMIDACVT TLIQGRLFER DIYFEKFISA ADAQQVRSPL FKRV
//
