DFA5_NOSS1
ID DFA5_NOSS1 Reviewed; 570 AA.
AC Q8Z0C1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative diflavin flavoprotein A 5;
DE EC=1.-.-.-;
GN Name=dfa5; OrderedLocusNames=all0177;
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, 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; BA000019; BAB77701.1; -; Genomic_DNA.
DR PIR; AI1828; AI1828.
DR RefSeq; WP_010994354.1; NZ_RSCN01000026.1.
DR PDB; 4FEK; X-ray; 2.00 A; A/B=1-254.
DR PDBsum; 4FEK; -.
DR AlphaFoldDB; Q8Z0C1; -.
DR SMR; Q8Z0C1; -.
DR STRING; 103690.17135155; -.
DR EnsemblBacteria; BAB77701; BAB77701; BAB77701.
DR KEGG; ana:all0177; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OMA; TIGGHAP; -.
DR OrthoDB; 1149616at2; -.
DR EvolutionaryTrace; Q8Z0C1; -.
DR Proteomes; UP000002483; 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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..570
FT /note="Putative diflavin flavoprotein A 5"
FT /id="PRO_0000216797"
FT DOMAIN 260..402
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 38..231
FT /note="Zinc metallo-hydrolase"
FT REGION 421..570
FT /note="Flavodoxin-reductase-like"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 41..56
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4FEK"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4FEK"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4FEK"
FT STRAND 225..236
FT /evidence="ECO:0007829|PDB:4FEK"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:4FEK"
SQ SEQUENCE 570 AA; 62573 MW; 81082F4333810558 CRC64;
MSDSKPRDVQ VLPIATNTKV LRARSWSRLR FEIEYALERG TTSNSYVIEG DKTAIIDPPV
ESFMKIYLEA LQQTVNLKKL DYVILGHFSP NRIPTFKALL ELAPQITFVC SLPAAGDLRA
AFPDDNLNIL PMRGKETLDL GKGHVLKFLP IPSPRWPAGL CTYDVQTQIL YTDKIFGAHI
CGDDVFDDNW ESFKEDQRYY FNCLMAPHAI HVEAALEKIS DLQVRLYAVG HGPLVRTSLI
ALTQAYADWS KAQKDREISV ALLYASAYGN TATIARAIAL GLTKGGVAVK SINCEFATPE
EIQTNLEQVD GFLIGSPTIG GHAPTPINTA LGIVLKVGDN NKLAGVFGSY GWSGEALDMI
EGKLRDAGYR FGLDTLKVKF KPDDVTLKFC EEVGTDFAQT LKKAKKVRVP QQAATPVEQA
VGRIVGSVCV ITAKQGDVST GMLGSWVSQA TFNPPGLTVA IAKERAIESL MYPGGKFALN
ILSEGNHLEY MKHFRKNFAP GEDRFANFTT TEADNGCTVL ADALAYVECS VDQRLECGDH
WVVYATVDNG KLLKPDDVTA INHRKTGNHY
