ID A1B5X1_PARDP Unreviewed; 358 AA.
AC A1B5X1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:ABL70915.1};
GN OrderedLocusNames=Pden_2831 {ECO:0000313|EMBL:ABL70915.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL70915.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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; CP000489; ABL70915.1; -; Genomic_DNA.
DR RefSeq; WP_011749106.1; NC_008686.1.
DR AlphaFoldDB; A1B5X1; -.
DR STRING; 318586.Pden_2831; -.
DR EnsemblBacteria; ABL70915; ABL70915; Pden_2831.
DR GeneID; 75502290; -.
DR KEGG; pde:Pden_2831; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_3_5; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000000361; Chromosome 1.
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; cd06215; FNR_iron_sulfur_binding_1; 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:SF6; NADH OXIDOREDUCTASE HCR; 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 Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 14..117
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 274..358
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 358 AA; 39056 MW; DCEF67517D5BBD2D CRC64;
MAVLVKAFGD RPWKDDEPLE CAMVVPETSD TATFTFRAPS GAYFDYQPGQ FVTLDLPVPG
GNVQRTYTIS SSPSRPLSIS VTVKAQPGSV GGRWMIDHLR PGMRLKAFGP AGIFSFVRHE
APKYLFISAG SGITPVMSMT TWAWDSGEMP DIVFVHAARA PADIIFRQRL EGMADRVPGL
QLRFAVEESD PFRTWHGYRG RLNQIMLGLM APDYLEREVF CCGPEPFMQA VRDMLIALGF
DMDHYHQESF GAPIRNEAEA PVLDDVVPDE ESAAQITFES SGVVAKCQET DTVLAVAKAN
GLNIPSGCTF GLCGTCKVRK TAGEVHMVHN GGITDEDIEE GYILACCSHP IGAVSVEV
//
