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Database: UniProt
Entry: A0A2A2IVV2_9PSED
LinkDB: A0A2A2IVV2_9PSED
Original site: A0A2A2IVV2_9PSED 
ID   A0A2A2IVV2_9PSED        Unreviewed;       794 AA.
AC   A0A2A2IVV2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Flavodoxin {ECO:0000313|EMBL:PAV47887.1};
GN   ORFNames=CK486_11400 {ECO:0000313|EMBL:PAV47887.1};
OS   Pseudomonas sp. HAR-UPW-AIA-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1985301 {ECO:0000313|EMBL:PAV47887.1, ECO:0000313|Proteomes:UP000243299};
RN   [1] {ECO:0000313|Proteomes:UP000243299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAR-UPW-AIA-41 {ECO:0000313|Proteomes:UP000243299};
RA   Kumari P., Krishnamurthi S.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:PAV47887.1}.
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DR   EMBL; NSLB01000005; PAV47887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2IVV2; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000243299; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR   CDD; cd06200; SiR_like1; 1.
DR   Gene3D; 3.40.50.360; -; 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; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR34219:SF3; BLL7967 PROTEIN; 1.
DR   PANTHER; PTHR34219; IRON-REGULATED INNER MEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243299};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          394..531
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          544..655
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          224..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  87679 MW;  B1DCC490EB736821 CRC64;
     MFKKIVFQLH WFFGISAGLV LVLMGVTGAL YAFEGEIMGA LNPEVLKVEV RDSGILPPAA
     LVAKIEAAEG KTVSGLWVDQ RDGQASRVFF TPPPGERRGP MRYFDPYTGE LLAQPSGQAF
     FGLMLKLHRF LAMGDTGKQI TAASTLALVF FCLSGLYLRW PRQALNWRAW LSLDWAKRGR
     AFNWDLHAVF GTWALLFYLC ASLTGLYWSY DWYRDGMTRL LSDAPAGEHR KPGEGRREGG
     RPGQQGVPSG QPPVVDYPAL WHSLQQAAGP QLAAWNLRLP PVAGQPATLF YLLEDAGHSR
     AFNQLTLETD RGRVLKHERY ADKTFGAQLL GSVYALHTGE YFGLLGRILM ALASLAMPLF
     AITGWLLYLD RRRKKKAVQA ARVATGEGGA GEPWLIGFAS QSGMAEQLAW RSAGQLQAAG
     HTVQVQPLAR LDAQKLQQAR RALFVVSTFG DGEAPDNARG FERKLLTGEL ALGELSYAVL
     ALGDRQYQQF CGFARRLHDW LGRQGARSLF SPVEVDNGDS ASLNRWQQQL VELGAAEATA
     EVAPDLQNWT LLERRCLNPG SSGSPLFLLR LQGPQDAQWK AGDLLQVQPG NETAAALRDY
     SIATLPAAGV LELLVRQERL SDGRLGLCSG WLTTDLALGG SLRASLRSNP AFRVPEADVP
     LILIGNGSGL AGLRSLLQAR VALGRQRNWL LFGERNREHD FFLREELEGY LADGHLQRLD
     LAFSRDQAEK VYVQDRLREA RVELLRWLEQ GAVLAVCGSL KGMAAGVDEV LLELLGREAF
     EQLQDSGRYR RDVY
//
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