DFA1_THEVB
ID DFA1_THEVB Reviewed; 571 AA.
AC Q8DJY2;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative diflavin flavoprotein A 1;
DE EC=1.-.-.-;
GN Name=dfa1; OrderedLocusNames=tlr1088;
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; BAC08641.1; -; Genomic_DNA.
DR RefSeq; NP_681879.1; NC_004113.1.
DR RefSeq; WP_011056931.1; NC_004113.1.
DR AlphaFoldDB; Q8DJY2; -.
DR SMR; Q8DJY2; -.
DR STRING; 197221.22294812; -.
DR EnsemblBacteria; BAC08641; BAC08641; BAC08641.
DR KEGG; tel:tlr1088; -.
DR PATRIC; fig|197221.4.peg.1142; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OMA; FGMHYCD; -.
DR OrthoDB; 1149616at2; -.
DR Proteomes; UP000000440; 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..571
FT /note="Putative diflavin flavoprotein A 1"
FT /id="PRO_0000216799"
FT DOMAIN 265..426
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 43..236
FT /note="Zinc metallo-hydrolase"
FT REGION 427..571
FT /note="Flavodoxin-reductase-like"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 62924 MW; E19ABF912595D9B0 CRC64;
MAVTITKRPP RLTLQVLDIA PETTAIRCLD WDRDRFDIEF ALENGTTYNS FLIKGERIAL
VDTSHAKFGD RYLEQLWQLV NPSDLDYLIV SHTEPDHSGL VKDVLVKAPH VTVVASKVAL
QFLGDLIHQP FTQQQVKNGD RLDLGKGHVL EFVMAPNLHW PDTILTFDHG TQTLFTCDVF
GAHFCNDDPF DSEPELLAPD FKFYYDCLMG PNARSVLSAF KRLESLPPVQ LVATGHGPLL
RHHLDQWLES YRNWSQEQAK AATTVAIFYA ANYGYSNALA EAIERGTAKT GVVVEKMDLL
TAEPQDIREL TEIAAGIIIG TPPTTAVAKT ALSTIRAAAH AKQAIGVFES GVADAEPAYP
LLNQFRDAGL VPSFPVIRVT AAPTDALFQE AEEAGTDMGQ WLLRDRTVKQ MKALDTDLDK
ALGRLSGGLY IITAQKGAIN SAMLASWVAQ ASTEPLGVSI AVAKDRAIES FLHVGDTFVL
NVLEAENYQP LMRHFLKRFP PGADRFAHVK TYPASNGSPI LADALAYMEC TVVSRLDAHD
HWIVYSTVDS GRVSKPDGMT AVHHRKVGNH Y
