DFA2_SYNY3
ID DFA2_SYNY3 Reviewed; 578 AA.
AC P72723;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative diflavin flavoprotein A 2;
DE EC=1.-.-.-;
GN Name=dfa2; OrderedLocusNames=sll0217;
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; BAA16730.1; -; Genomic_DNA.
DR PIR; S74578; S74578.
DR AlphaFoldDB; P72723; -.
DR SMR; P72723; -.
DR IntAct; P72723; 1.
DR STRING; 1148.1651803; -.
DR PaxDb; P72723; -.
DR EnsemblBacteria; BAA16730; BAA16730; BAA16730.
DR KEGG; syn:sll0217; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR InParanoid; P72723; -.
DR OMA; FGMHYCD; -.
DR PhylomeDB; P72723; -.
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 3: Inferred from homology;
KW Electron transport; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..578
FT /note="Putative diflavin flavoprotein A 2"
FT /id="PRO_0000216802"
FT DOMAIN 269..406
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 48..240
FT /note="Zinc metallo-hydrolase"
FT REGION 429..578
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 578 AA; 64083 MW; 88F0FF9E5EF7C938 CRC64;
MVTLIDSPTS AAVQPRLTLQ TADIAAHTTA IRCLDWDRDR FDIEFELRHG TTYNSFLIRG
EKTALIDTSH RKFEAVYLQL LQDLVDLRSL DYLIVNHTEP DHSGLIPDLL ELAPQVTVVG
SKVAIQFLEK LVHRPFESQI VKSGHSLDLG QGHELQFISA PNLHWPDTIL TYDSGTQVLY
TCDVFGMHYC DDSLFDETPE RLEPDFQYYY NCLMGSNARS VLMALKRIAP LQVVLVATGH
GPLLQHHISH WLGQYDAWSQ NQVKAETFVA LFYVDGYGVS DRLVQTIADG ISKTGVAIEL
VDLSVADTHE VRTLAQCAAG LVVGMPPQSS TSTTLDPLLG TILAAVHPKQ VIGLFESGGG
QDEPIYPLRN RFQELGLQEA FEPILLKTEP TAATDQLCRE AGTDLGQYLT QKQSQQANTD
LDPELNQAIG RLSTGLYILT AQKGDVRSAM LASWVIQGSF EPLGIVIAVA KDRAIESLLH
PGDTFVLNVL EEDNYQSLMR HFLLRFPPGA DRFAGVNTYP AQNGSPILLE TLAYLECEVT
SRLDGNDHWL VYSTIQTGRV AKLNALTATH HRKLGNHY
