DFA3_NOSS1
ID DFA3_NOSS1 Reviewed; 574 AA.
AC Q8YQD8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative diflavin flavoprotein A 3;
DE EC=1.-.-.-;
GN Name=dfa3; OrderedLocusNames=all3895;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- FUNCTION: Mediates electron transfer from NADH to oxygen, reducing it
CC to water. This modular protein has 3 redox cofactors, in other
CC organisms the same activity requires 2 or 3 proteins (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per subunit.;
CC -!- MISCELLANEOUS: By homology with NorV in E.coli, could be involved in
CC nitric oxide detoxification. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavodoxin
CC reductase family. {ECO:0000305}.
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DR EMBL; BA000019; BAB75594.1; -; Genomic_DNA.
DR PIR; AH2292; AH2292.
DR RefSeq; WP_010998036.1; NZ_RSCN01000011.1.
DR PDB; 2KLB; NMR; -; A=264-409.
DR PDB; 3FNI; X-ray; 2.30 A; A=259-409.
DR PDBsum; 2KLB; -.
DR PDBsum; 3FNI; -.
DR AlphaFoldDB; Q8YQD8; -.
DR BMRB; Q8YQD8; -.
DR SMR; Q8YQD8; -.
DR STRING; 103690.17133029; -.
DR PRIDE; Q8YQD8; -.
DR EnsemblBacteria; BAB75594; BAB75594; BAB75594.
DR KEGG; ana:all3895; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OMA; AFGLHYC; -.
DR OrthoDB; 1149616at2; -.
DR EvolutionaryTrace; Q8YQD8; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR Gene3D; 2.30.110.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..574
FT /note="Putative diflavin flavoprotein A 3"
FT /id="PRO_0000216795"
FT DOMAIN 265..409
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 43..236
FT /note="Zinc metallo-hydrolase"
FT REGION 410..574
FT /note="Flavodoxin-reductase-like"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2KLB"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:3FNI"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:3FNI"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3FNI"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:3FNI"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3FNI"
FT HELIX 388..409
FT /evidence="ECO:0007829|PDB:3FNI"
SQ SEQUENCE 574 AA; 63513 MW; F2BF5554AA332C23 CRC64;
MVALTEKTEK RLTIQTADIA QDTTAIRSLD WERDRFDIEF GLQNGTTYNS FLIRGEQIAL
VDTSHEKFRQ LYFDTLTGLI NPTEINYLII SHTEPDHSGL VKDLLQMAPE ITVVGSKVAI
QFLEDLVHQP FKRKIVKNGD RLDLGNGHEF EFVIAPNLHW PDTIFSFDHK TQTLYTCDAF
GMHYCSDIVF DEDLKTIEPD FHYYYDCLMG PNARSVLSAL KRMGELPSVK MIATGHGPLL
YHNVEELTGR YRTWSQNQTK AETSIGVFYV SEYGYSDRLA QAIINGITKT GVGVDVVDLG
AAVDLQELRE LVGRCTGLVI GMSPAASAAS IQGALSTILG SVNEKQAVGI FETGGGDDEP
IDPLLSKFRN LGLTTAFPAI RIKQTPTENT YKLCEEAGTD LGQWVTRDRS IKAMKSLGAD
LDKALGRLSG GLYIITAKKG DVSSAMLASW VNQASFKPLG FSIAVAKDRA IESLMQVGDR
FVLNVLEEGN YQPLMRHFLK RFAPGADRFE GVKTQPAENG APILGDALAY MECEVVSRMD
CGDHWAVYST VYAGRVSKSE ALTAVHHRKV GNHY
