ID   DFA2_THEVB              Reviewed;         578 AA.
AC   Q8DJ55;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative diflavin flavoprotein A 2;
DE            EC=1.-.-.-;
GN   Name=dfa2; OrderedLocusNames=tll1373;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(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 (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; BA000039; BAC08925.1; -; Genomic_DNA.
DR   RefSeq; NP_682163.1; NC_004113.1.
DR   RefSeq; WP_011057213.1; NC_004113.1.
DR   AlphaFoldDB; Q8DJ55; -.
DR   SMR; Q8DJ55; -.
DR   STRING; 197221.22295097; -.
DR   EnsemblBacteria; BAC08925; BAC08925; BAC08925.
DR   KEGG; tel:tll1373; -.
DR   PATRIC; fig|197221.4.peg.1442; -.
DR   eggNOG; COG0426; Bacteria.
DR   eggNOG; COG1853; Bacteria.
DR   OMA; PEAPIYC; -.
DR   OrthoDB; 1149616at2; -.
DR   Proteomes; UP000000440; 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..578
FT                   /note="Putative diflavin flavoprotein A 2"
FT                   /id="PRO_0000216800"
FT   DOMAIN          262..404
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   REGION          39..233
FT                   /note="Zinc metallo-hydrolase"
FT   REGION          429..578
FT                   /note="Flavodoxin-reductase-like"
SQ   SEQUENCE   578 AA;  63433 MW;  C8FD454091B8AAFE CRC64;
     MLTETRPRDV QVAEIAPGVL VLRSRTWDRL KFEVEYGRQQ GTTSNSYLIQ APQPALLDPP
     GESFTQIYLQ ELQRHIDLNQ LRYLILSHVN SNRLATVKVL LEKAPQITLV CSKAGAVTLR
     SAIGEQLHLW IARADTPLEL GGDRQLMFIA AATPRWPDGL ITVDPQNQIV FSDKLFGAHV
     CGDSLYDEQW KKLDEDRAYY FECLHAAQTR QVESILDRLA ELTPPPRLYA PAHGPIVKFS
     RSRLFQDYRD WCQAQAEQET KVALFYASAY GNTAILANAI AQGLTAAGVQ VEAVNCETTP
     PAEMQALIHS SDGFIIGSPT LGGHMPTQVQ TALGFILAEG SQTKLAGVFG SYGWSGEAID
     DIEQKLLDAG YTLGFETLRV KFTPTATDLE KCQIAANEFA QALKKLRKSR TVRPSSLAEA
     QVDRTEQAVN RVVGSLCVLT TLPEGCFHLT QAAAILVSSV SQASFNPPGI TVSLPQEWAE
     SLCLVGDRFV LNILKEGSPL VRQFQQAQRL GEQQLATLGL KSAESGAPIL LDALAYLECT
     VESRMNCGNH WLIYAVVESG ELLQTSGLTA IQHRKTSS