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
//