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Database: UniProt
Entry: A0A2I0CPD5_9PSED
LinkDB: A0A2I0CPD5_9PSED
Original site: A0A2I0CPD5_9PSED 
ID   A0A2I0CPD5_9PSED        Unreviewed;       323 AA.
AC   A0A2I0CPD5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:PKF70933.1};
GN   ORFNames=CW360_10455 {ECO:0000313|EMBL:PKF70933.1};
OS   Pseudomonas pharmacofabricae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1905276 {ECO:0000313|EMBL:PKF70933.1, ECO:0000313|Proteomes:UP000242861};
RN   [1] {ECO:0000313|Proteomes:UP000242861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZYSR67-Z {ECO:0000313|Proteomes:UP000242861};
RA   Yu X.-Y.;
RL   Submitted (DEC-2017) 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:PKF70933.1}.
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DR   EMBL; PIYS01000018; PKF70933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0CPD5; -.
DR   Proteomes; UP000242861; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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; IPR012675; Beta-grasp_dom_sf.
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; 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; 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:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242861}.
FT   DOMAIN          2..84
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          91..189
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   323 AA;  34999 MW;  DEF54EAEF794A1B7 CRC64;
     MLKVTLQPSG LVLQVEQGER ILDAARRQGV ECPQSCRNGN CRICAALLVN GRIRQAGQSL
     EQGEVFSCLA VPEEDCVLHW EGVLAPGELP VRRLACQVLG CEPLGGDVYR VQLRAPAGKP
     LRYHAGQYLL VERADGDMAA FSIASAPHQG RELELHILVR EESTRQLLAQ LQQQGTVSVQ
     LPMGSVQLRE PAPAGLLLIA AGTGLAQMHS LVAHSLAQGW TQPIHLYWGV RQATDFYALP
     ALAAWQASGQ VRVHQVVSDD PAWAGRQGLL HEAVCADFAD FRGLQVYASG SPGMVYATLD
     ALLAAGMQRE QMQADVFDYA PRD
//
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