DFA2_NOSS1
ID DFA2_NOSS1 Reviewed; 579 AA.
AC Q8Z0C0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative diflavin flavoprotein A 2;
DE EC=1.-.-.-;
GN Name=dfa2; OrderedLocusNames=all0178;
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; BAB77702.1; -; Genomic_DNA.
DR PIR; AB1829; AB1829.
DR RefSeq; WP_010994355.1; NZ_RSCN01000026.1.
DR AlphaFoldDB; Q8Z0C0; -.
DR SMR; Q8Z0C0; -.
DR STRING; 103690.17135156; -.
DR EnsemblBacteria; BAB77702; BAB77702; BAB77702.
DR KEGG; ana:all0178; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OMA; YIIVSHT; -.
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..579
FT /note="Putative diflavin flavoprotein A 2"
FT /id="PRO_0000216794"
FT DOMAIN 272..460
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 50..243
FT /note="Zinc metallo-hydrolase"
FT REGION 461..579
FT /note="Flavodoxin-reductase-like"
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="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 579 AA; 64283 MW; 0DD930EBBDC68F00 CRC64;
MVSMSTTGNA HTENVQHRLT VETVEIAPNT TAIRCLDWDR DRFDIEFGLQ NGTTYNSYLI
RGEQTVLVDT SHQKFRQLYL ETLKGLINPK AIDYIIVSHT EPDHSGLVED VLQLAPRATV
LASKIALQFL EGLVHDPFSK RIVKSGDRID IGKGHEIEFV SAPNLHWPDT IFSYDRKTEV
IYTCDAFGMH FCDNRTFDED LEAIEADFRF YYDCLMGPNA RSLLNAMKRM GDLGKIKIIA
NGHGPLLYHH LDVLTECYQS WSQRQAKSET TVGLFYVADY GYSNLLVQAI GEGIQKTGVA
VEMIDLSTAE IQEIQELAGR AAGLIIGMPP TTSVAAQAGI SSLLSVVKDK QAVGLFECFG
GDDEPVDTIR RKFIDLGVKE AFPAIRIKDV PGASAYQLCT EAGTDLGQLL TRERNIKQIK
SLDVNMEKAL GRISNGLYIV TTKKGDVSSA MLASWVSQAS LQPLGFTIAV AKDRAIDSLM
QVGDRFVLNV LEEGNYQELK KQFLKRLHPG ADRFAGVRTQ TAKNGSPILT DALAYMECEI
QSSLECSDHY ILYCTVEDGR VSKPDGLTAV RHRKVGNYY
