ID T0IAG0_9SPHN Unreviewed; 641 AA.
AC T0IAG0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Flavodoxin {ECO:0000313|EMBL:EQB06594.1};
GN ORFNames=L485_00250 {ECO:0000313|EMBL:EQB06594.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB06594.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQB06594.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQB06594.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EQB06594.1}.
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DR EMBL; ATIB01000014; EQB06594.1; -; Genomic_DNA.
DR AlphaFoldDB; T0IAG0; -.
DR PATRIC; fig|1114964.3.peg.34; -.
DR eggNOG; COG1018; Bacteria.
DR Proteomes; UP000015524; 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; cd06217; FNR_iron_sulfur_binding_3; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PR00371; FPNCR.
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:UP000015524};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..641
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004564292"
FT DOMAIN 285..391
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 556..641
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 28..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 67334 MW; 8D02519FAC60719B CRC64;
MCVWTSLRLS GLGLLLAFSL PSASVHAQEG EDHSAHHGDT SGGAGMADGA MSAKPEVGTS
DMASMMNSMM ERMINGEGEN EHGHDSRRTA FFSQLLAFPA LDEAARQRVA AQAGERVSTG
LSMVNAASAD GARATTVSAR LDAARRMREG TDLFRSGTAA QGAIGGLQPP REVGLAWLRD
QLDIDQAAPG HADHWFGISP SHLLLMLFLG LVSATLIALQ IFRLRRIGAI AGGVATAKVP
AKPEPKAAPP ATRVAPAPAP VADSAGLAPS NAAAPAGASL RKPKSWAGQL RVVQIVRETP
SVLTFRLADP TADRLPFDFL PGQFLQVEVE PEAGKTARRS YTIASSPTQR AYVELTVKRE
EQGVVSRYLH DKVVADDLLK VSGPFGAFTF TGTDAQSIVL IAGGVGITPM MSVLRYLTDT
AWKGDIFFFY GARSTEEFVF RDELERLERR FPNLHVVAAM QRAPGTVWMG PEGPITREMI
LAAVPEIASR RIHMCGPPAM MGAMRGVLAE LGVPEAQLHT EAFGPASLPA DHEDLEVKPA
PAPADKPAPS AEVAPSTVTF SVSGVSAALP ADETVLEAAE GAGVEISYAC RAGTCGACVV
KLLQGEVTME VESGLAPADK AQGYVLACQA KGTGTPLVVE A
//
