ID Q1NBR0_SPHSS Unreviewed; 636 AA.
AC Q1NBR0;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Flavodoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=SKA58_18920 {ECO:0000313|EMBL:EAT08543.1};
OS Sphingomonas sp. (strain SKA58).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT08543.1, ECO:0000313|Proteomes:UP000005395};
RN [1] {ECO:0000313|EMBL:EAT08543.1, ECO:0000313|Proteomes:UP000005395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT08543.1,
RC ECO:0000313|Proteomes:UP000005395};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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:EAT08543.1}.
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DR EMBL; AAQG01000009; EAT08543.1; -; Genomic_DNA.
DR RefSeq; WP_009824016.1; NZ_CH959309.1.
DR AlphaFoldDB; Q1NBR0; -.
DR STRING; 314266.SKA58_18920; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_420255_0_0_5; -.
DR OrthoDB; 9786134at2; -.
DR Proteomes; UP000005395; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000005395};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..636
FT /note="Flavodoxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004195004"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 280..386
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 551..636
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 66486 MW; E2396881C3434B9B CRC64;
MSRRISLRRL SLGCAIALSL SAGAGAQEGE DHAAHHGAGM PAGGGMSAPA SSGSSDMAKM
MNPMMDRMIN GEGENEHGHE SRRTGFISQL LAFPALDEAA RQRVAAQAGE RVSTGLAMIN
AASADGARAT TVSARLDAAR RLREGTDLFR SGTAAQGAIG GLQPPREVGL AWLRDQLDID
QAAPGHADHW FGISPSHLLL MLFLGLVSAT LIALQIFRLR RIGAIAGGVA TAKTSEKPEP
KAVPPAAKLA PAPAPVAGSA GLASSNAAAP AGASLRKPKS WAGQLRVVQI VRETPSVLTF
RLADPAADRL PFDFLPGQFL QVEVEPEAGK TARRSYTIAS SPTQRAYVEL TVKREEQGVV
SRYLHDKVVA DDLLKVSGPF GAFTFTGTDA QSIVLIAGGV GITPMMSVLR YLTDTAWKGD
IFFFYGARST EEFVFRDELE RLERRFPNLH VVAAMQRAPG TVWMGPEGPI TREMILAAVP
EIASRRIHMC GPPAMMGAMR GVLAELGVPE AQLHTEAFGP ASLPADHEDL EVKPAPAPAA
KPAPSAEVAP STVTFSVSGV SAALPADETV LEAAEGAGVE IPYACRAGTC GACVVKLLQG
EVTMEVESGL APADKAQGYV LACQAKGTGT PLVVEA
//
