ID A9BMY7_DELAS Unreviewed; 461 AA.
AC A9BMY7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Flavodoxin/nitric oxide synthase {ECO:0000313|EMBL:ABX37682.1};
GN OrderedLocusNames=Daci_5053 {ECO:0000313|EMBL:ABX37682.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX37682.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX37682.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP000884; ABX37682.1; -; Genomic_DNA.
DR RefSeq; WP_012206852.1; NC_010002.1.
DR AlphaFoldDB; A9BMY7; -.
DR STRING; 398578.Daci_5053; -.
DR GeneID; 24114999; -.
DR KEGG; dac:Daci_5053; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_001570_17_7_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..192
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 206..318
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 461 AA; 50372 MW; 1475B0914C24C965 CRC64;
MTLSETGLRV LAAAVLVLLY AAMCAAIWWR ERRQRMRARQ EAAALTSARE GALPLLVAYA
SQTGQAEELA RETARLLHTA GESVHLCALD AVDADLLART QRALFIASTY GEGDPPDNAA
LFLAHAMAQA QDLSHLQYGL LALGDRQYAQ FCGYGRALDS WLRAGGARPW FERIEMDNGA
PQALTAWQHQ LTQISSLGDM PAWEQPVFSE WTLAARRHMN PRSAGEPVFH IELQPPATEP
ALWESGDLAQ VCIPADPQHP REYSIASIAQ DGCVHLLVRQ ARREDGSPGL ASGWLTQGAP
LGAAITLRLR AHRNFRLEDN LQRPLVLIGN GTGLAGLRSH LRARAAAGLG PNWLLFGERN
AAHDRLYGDE LQAWCDGGVL QRLDLAFSRD RSEGAPRAYV QDLLAQSGDV LRQWVAQGAA
IYVCGSLQGM AQGVDQALHA VLGEAQMELL VCSGRYRRDV Y
//
