DFA1_NOSS1
ID DFA1_NOSS1 Reviewed; 576 AA.
AC Q8YNW5;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative diflavin flavoprotein A 1;
DE EC=1.-.-.-;
GN Name=dfa1; OrderedLocusNames=all4446;
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; BAB76145.1; -; Genomic_DNA.
DR PIR; AF2361; AF2361.
DR RefSeq; WP_010998579.1; NZ_RSCN01000054.1.
DR AlphaFoldDB; Q8YNW5; -.
DR SMR; Q8YNW5; -.
DR STRING; 103690.17133582; -.
DR EnsemblBacteria; BAB76145; BAB76145; BAB76145.
DR KEGG; ana:all4446; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OMA; FGMHYCD; -.
DR OrthoDB; 1149616at2; -.
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 3: Inferred from homology;
KW Electron transport; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..576
FT /note="Putative diflavin flavoprotein A 1"
FT /id="PRO_0000216793"
FT DOMAIN 269..431
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 48..240
FT /note="Zinc metallo-hydrolase"
FT REGION 432..576
FT /note="Flavodoxin-reductase-like"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 64088 MW; AC885FEFEB8C694D CRC64;
MVALTEDTQA NANIGRLTVQ TVEIADETTA IRCLDWDRER FDIEFGLRNG TTYNSFLIKG
EKIALVDTSH RKFEKLYLEI VAGLIDPNTI DYLIVSHTEP DHSGLVKDIL QLAPNITIVG
AKVAIQFLEN MVHQPFKSLQ VKSGERLDLG NGHSLEFVSA PNLHWPDTIL TYDHKTGILY
TCDVFGMHYC DDQTYDENFF AIEEDFKYYY DCLMGPNARS VLAALKRIEN LAIKTVATGH
GPLLQVHISE WLGRYKNWSL EQAKTETLVA LFYAEDYGYS EHLVHILGHG CTKTGVAVEL
IDLNTAEPQE VRELVTQASG LVIAMPSQYS LTAQAALNTI LAAVHHKQAI GLLESGGGED
EPVFPLRNKF QELGLVEAFP PILIKEAPAQ TTEQLCEEAG TDIGQWLTRD RTIKQIKSIN
TDLEKALGRI STGLYIITTK KGEIQGAMFA SWVTQASLNP LGVAIAVSKE RAIESLMQVG
DHFVLNVLEE DNYQGLMKHF LKRFAPGADR FAGIKTYPAT DGSPILAESL AYTECEITSR
MDCGDHWIIY STVHVGRVAN VHAMTAVHHR KVGNHY
