DFA1_SYNY3
ID DFA1_SYNY3 Reviewed; 573 AA.
AC Q55393;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Diflavin flavoprotein A 1;
DE EC=1.-.-.-;
DE AltName: Full=NADH:oxygen oxidoreductase;
DE AltName: Full=SsATF573;
GN Name=dfa1; OrderedLocusNames=sll0550;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9660187; DOI=10.1046/j.1432-1327.1998.2540325.x;
RA Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.;
RT "A family of flavoproteins in the domains Archaea and Bacteria.";
RL Eur. J. Biochem. 254:325-332(1998).
RN [4]
RP CHARACTERIZATION.
RX PubMed=12054744; DOI=10.1016/s0006-291x(02)00434-5;
RA Vicente J.B., Gomes C.M., Wasserfallen A., Teixeira M.;
RT "Module fusion in an A-type flavoprotein from the cyanobacterium
RT Synechocystis condenses a multiple-component pathway in a single
RT polypeptide chain.";
RL Biochem. Biophys. Res. Commun. 294:82-87(2002).
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.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per monomer.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: By homology with NorV in E.coli, may 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; BA000022; BAA10483.1; -; Genomic_DNA.
DR PIR; S75748; S75748.
DR AlphaFoldDB; Q55393; -.
DR SMR; Q55393; -.
DR IntAct; Q55393; 1.
DR STRING; 1148.1001242; -.
DR PaxDb; Q55393; -.
DR EnsemblBacteria; BAA10483; BAA10483; BAA10483.
DR KEGG; syn:sll0550; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR InParanoid; Q55393; -.
DR OMA; AFGLHYC; -.
DR PhylomeDB; Q55393; -.
DR Proteomes; UP000001425; 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 Electron transport; FAD; Flavoprotein; FMN; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..573
FT /note="Diflavin flavoprotein A 1"
FT /id="PRO_0000216801"
FT DOMAIN 265..401
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 43..236
FT /note="Zinc metallo-hydrolase"
FT REGION 424..573
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"
SQ SEQUENCE 573 AA; 63506 MW; E31BE51028949E58 CRC64;
MFTTPLPPQK RLSTQTEAIA KNITAIRSLD WDRDRFDIEF GLQNGTTYNS YLIQADKVAL
VDSSHEKFRQ LYLDLLQGLI DPQRIDYLIV SHTEPDHSGL VKDILQLNPR ITVVATKVAL
QFLDNFVHQP FERIQVKSGD RLDLGQGHDL EFVSAPNLHW PDTMLTYDPA TEILFTCDVF
GMHYCSDAVF DIDLGKIAPD YQFYYDCLMG PNARSVLAAM KRMDNLGTIS TVANGHGPLL
RHNVGELLHR YRHWSESQSK AEKTVVVFYV ADYGYGDRLS QAIAKGITKT GVGVDMVDLS
SADPQEIQEL VGHASGVVLG MPPLQANADL STNFGAVLAA MQPKQVFGLY ESYGGDDEPI
DPLRTKFLDL GLREAFKVIK VKDTPSESTY QLCDESGTDL GQNLIQAAKI KQLKSLDSDL
EKAIGRISGG LYIITAQKGE VKGAMLASWV SQASFNPPGF TVAVAKDRAI ESLMQVGDRF
VLNILEEGNY QILMKHFLKR FPPGADRFAG VKTQTASNGS PILTDALAYL ECEVASRMEC
SDHWIVYSQV TNGRVAKAEG LTAVHHRKVG NYY
