ID   DFA4_SYNY3              Reviewed;         594 AA.
AC   P72721;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Putative diflavin flavoprotein A 4;
DE            EC=1.-.-.-;
GN   Name=dfa4; OrderedLocusNames=sll0219;
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=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).
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, 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; BAA16728.1; -; Genomic_DNA.
DR   PIR; S74576; S74576.
DR   AlphaFoldDB; P72721; -.
DR   SMR; P72721; -.
DR   STRING; 1148.1651801; -.
DR   PaxDb; P72721; -.
DR   PRIDE; P72721; -.
DR   EnsemblBacteria; BAA16728; BAA16728; BAA16728.
DR   KEGG; syn:sll0219; -.
DR   eggNOG; COG0426; Bacteria.
DR   eggNOG; COG1853; Bacteria.
DR   InParanoid; P72721; -.
DR   OMA; PEAPIYC; -.
DR   PhylomeDB; P72721; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; IPR001226; Flavodoxin_CS.
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; PF00258; Flavodoxin_1; 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; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..594
FT                   /note="Putative diflavin flavoprotein A 4"
FT                   /id="PRO_0000216804"
FT   DOMAIN          279..417
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   REGION          57..250
FT                   /note="Zinc metallo-hydrolase"
FT   REGION          445..594
FT                   /note="Flavodoxin-reductase-like"
SQ   SEQUENCE   594 AA;  65597 MW;  70CD60E725BBED2D CRC64;
     MISPIGGLSQ ALHSPSDSIF VASLPRDIQV AEIAPQTKVL RSRLWDRLKF EVEYGRRRGT
     TSNSYLIQAD HTALIDPPGE SFCDLYLAEL PKYLDLAQLD YIVASHVNPN RMVTLEQLLR
     RATKAKLICS RPAAKVLKAT FPHWEERFQT VRSQDMLDLG RGHKLQLMTL PTPRWPDGLC
     AYDAGSQILF SDKLFGTHVC GDAIFDEDWR QLGGDRRFYF DCLHAPQTRQ VETALDQFDP
     LTLKMIAPGH GPLVRFSLSR LYSDYRQWCQ QQPSQTLKVA LIYASAYGNT ATMARAIAQG
     LVKAGVAVET INCEIAEPNE IVEAIQACDG FIVGSPTLGS HAPVQIQTAL GIVLSSATKT
     KLAGVFGSYG WSGEAIDLIE NKLKDGGYRF GFEAIRIQFS PNLDALDVCT TSGANFARQL
     RTHKRQRIAR QATTETQADR TQQAVGRIIG SIGVVTTQTT GRHQGILTSW VSQASFTPPG
     IMLAIPGEFD AYGLAGQNKA FVLNLLQEGR SVRRHFDHQP LPKDGDNPFS RLEHYSTQNG
     CLILAEALAY LECLVQSWSN IGDHVLVYAT VQAGQVLQPN GITAIRHRKS GGQY