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Database: UniProt
Entry: B0KMS6_PSEPG
LinkDB: B0KMS6_PSEPG
Original site: B0KMS6_PSEPG 
ID   B0KMS6_PSEPG            Unreviewed;       455 AA.
AC   B0KMS6;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ABY99530.1};
GN   OrderedLocusNames=PputGB1_3639 {ECO:0000313|EMBL:ABY99530.1};
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY99530.1, ECO:0000313|Proteomes:UP000002157};
RN   [1] {ECO:0000313|EMBL:ABY99530.1, ECO:0000313|Proteomes:UP000002157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1 {ECO:0000313|EMBL:ABY99530.1,
RC   ECO:0000313|Proteomes:UP000002157};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP000926; ABY99530.1; -; Genomic_DNA.
DR   RefSeq; WP_012273241.1; NC_010322.1.
DR   AlphaFoldDB; B0KMS6; -.
DR   KEGG; ppg:PputGB1_3639; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
FT   DOMAIN          32..65
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   455 AA;  48887 MW;  66F2859333A4ECD9 CRC64;
     MIDALNHLPR PRAGADQLAE RFSDLAPPLT ARQAAVESAR CLYCYDAPCV NACPSDIDIP
     SFIHRISDEN LQGAAERILS ANILGGSCAR VCPTEILCQQ ACVRNNAQEC APVLIGQLQR
     YALDNAQFSE HPFKRSPATG KRIAVVGAGP AGLSCAHRLA MHGHDVVVFE ASDKAGGLNE
     YGIARYKLVD DYAQREVEFL LGIGGIEVRH GQRLGGNLSL GELRDQYDAV FLGLGLNAVR
     QLGLPDEEAP GVLAATEYIR ELRQADDLSQ LPLADRCLVI GAGNTAIDMA VQMSRLGARD
     VNLVYRRGHA DMGATGHEQD IAKANQVRLH TWARPDAVLL DDAGKVRGMR FARTELADGR
     LRDTGETFEL AADAIFKAIG QRFDEASLGD PVAAQLARDG ERIRVDETMQ TSLPGVYAGG
     DCTALGQDLT VQAVQHGKLA AEAIHAQLML NVEAA
//
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