ID A0A2A4I3Z0_9SPHN Unreviewed; 636 AA.
AC A0A2A4I3Z0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Flavodoxin {ECO:0000313|EMBL:PCG13195.1};
GN ORFNames=COA07_15950 {ECO:0000313|EMBL:PCG13195.1};
OS Sphingomonas adhaesiva.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28212 {ECO:0000313|EMBL:PCG13195.1, ECO:0000313|Proteomes:UP000218323};
RN [1] {ECO:0000313|EMBL:PCG13195.1, ECO:0000313|Proteomes:UP000218323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7418 {ECO:0000313|EMBL:PCG13195.1,
RC ECO:0000313|Proteomes:UP000218323};
RA Feng G., Zhu H.;
RT "Sphingomonas adhaesiva DSM 7418, whole genome shotgun sequence.";
RL Submitted (SEP-2017) 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:PCG13195.1}.
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DR EMBL; NWVC01000011; PCG13195.1; -; Genomic_DNA.
DR RefSeq; WP_066708086.1; NZ_NWVC01000011.1.
DR AlphaFoldDB; A0A2A4I3Z0; -.
DR Proteomes; UP000218323; 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:UP000218323};
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 /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013195536"
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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 66703 MW; C038EBE0CD51899E CRC64;
MSRRISLRRL SLGCAIALSL SAGAGAQEGE DHAAHHGAGM PAGGGMSAPA SSGSSDMAKM
MKPMMDRMIN GEGENEHGHE SRRTGFISQL LAFPALDEAA RQRVAAQAGE RVSTGLAMIN
AASADGARAT TVSARLDAAR RLREGTDLFR SGTAAQGAIG GLQPPREVGL AWLRDQLDID
QAAPGHADHW FGISPSHLLL MLFLGLVSAT LIALQIFRLR RIGAIAGGVP TGKTLTKPEP
KAAQPATRVA PAPAPVDDSA GLAPSNAAAP 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 EVKPAPAPAD
KPAPSAEVAP STVTFSVSGV SAALPADETV LEAAEGAGVE ISYACRAGTC GACVVKLLQG
EVTMEVESGL APADKAQGYV LACQAKGTGT PLVVEA
//
