DFA3_SYNY3
ID DFA3_SYNY3 Reviewed; 597 AA.
AC P74373;
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 3;
DE EC=1.-.-.-;
GN Name=dfa3; OrderedLocusNames=sll1521;
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; BAA18468.1; -; Genomic_DNA.
DR PIR; S76209; S76209.
DR PDB; 6H0C; X-ray; 1.59 A; A=26-431.
DR PDB; 6H0D; X-ray; 1.60 A; A=26-428.
DR PDBsum; 6H0C; -.
DR PDBsum; 6H0D; -.
DR AlphaFoldDB; P74373; -.
DR SMR; P74373; -.
DR IntAct; P74373; 1.
DR STRING; 1148.1653555; -.
DR PaxDb; P74373; -.
DR EnsemblBacteria; BAA18468; BAA18468; BAA18468.
DR KEGG; syn:sll1521; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR InParanoid; P74373; -.
DR OMA; HVKNNIH; -.
DR PhylomeDB; P74373; -.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..597
FT /note="Putative diflavin flavoprotein A 3"
FT /id="PRO_0000216803"
FT DOMAIN 283..421
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 59..254
FT /note="Zinc metallo-hydrolase"
FT REGION 449..597
FT /note="Flavodoxin-reductase-like"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 62..77
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6H0C"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 365..375
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:6H0C"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:6H0C"
FT HELIX 407..429
FT /evidence="ECO:0007829|PDB:6H0C"
SQ SEQUENCE 597 AA; 65093 MW; D00B4E6D19FD0B1C CRC64;
MGIHAKLETV QLPLLVSCLF PPLTMPAKDV QICPIAVDTT VFRSRTWDRL KFEIEYGLQR
GTTANSYLIS ADKIALFDPP GESFTDNFVG TLIQRLDLNS LDYVILGHVN ANRAHTLKLL
LSLAPQATII CSNPAAQNLE KLLADAEVNN PIQVMKGNDH LDLGRGHELT FIPTPSPRYP
GQLCTYDPRT EILFTDKLFG AHVCGDQVFD EGWTIYQEDR RYYFDCLLAP AAAQVSAALN
KLEAYPAQTY APSHGPLVRY GLRELTRNYQ QWLSEQQAQA LNVALIYASA YGNTSTLAQA
IARGITKAGV AVTAINAETS NAEEIKEAIG KSAGFIFGSP TLGGHAPTPI QTALGITLAN
ASKTQLCGVF GSFGWSGEAI DMLENKFRDA GFSFGFDTIR VKFKPTDQTL KMCEEAGTDF
AQALKKAEKR RQPKSALPES ESARTEQALG RLVGSLCVVT AQQGELSSAM LASWVSQATF
SPPGLTVAVA KERAIESLLH KNSCFVLNIL QEGNHLGLMK HFLKPFAPGG DRFADVATET
AENGAPILTE SLAYLECRVQ QRLECGDHWV LYAVTDRGAL LKDGVTAVHH RKSGDHY
