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Database: UniProt
Entry: T0JB57_9SPHN
LinkDB: T0JB57_9SPHN
Original site: T0JB57_9SPHN 
ID   T0JB57_9SPHN            Unreviewed;       327 AA.
AC   T0JB57;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Ferredoxin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L284_02665 {ECO:0000313|EMBL:EQB19154.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB19154.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB19154.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB19154.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(2013).
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:EQB19154.1}.
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DR   EMBL; ATHL01000024; EQB19154.1; -; Genomic_DNA.
DR   RefSeq; WP_021232506.1; NZ_ATHL01000024.1.
DR   AlphaFoldDB; T0JB57; -.
DR   PATRIC; fig|1096930.3.peg.522; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9786134at2; -.
DR   Proteomes; UP000015527; 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; cd06185; PDR_like; 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; 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:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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:UP000015527}.
FT   DOMAIN          3..112
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          240..327
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   327 AA;  35146 MW;  D981C04846E784F6 CRC64;
     MHGQLIDMVV ADVRQLTPRI REYLLASADG SPLPRGAPGA HVELHTHSDH SGPIVRHYSL
     VGGLGLADDR ADHYRIAVQR EDRQRGSAHI HDTFAPGTRL KVSRPKNNFP LDLRDRRSLL
     IAGGIGITPI YAMLRSLARR GRPFELVYAG RMQAQLAYAA EAMELAGAAG RLHISGDPAT
     EHLDLAALLA AQSDDTAVYV CGPLPMIEAV HGAARTLGWP DARVRSERFT AGPAPDDAPF
     AVELRRTGRT VEVGRDTSIL DALTASGIDV LSDCRRGECG LCPLPVLEGG ERISHRDSYL
     SDEERAGGDT LCICVSRVPG GTLVLDA
//
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