ID DFA4_NOSS1 Reviewed; 575 AA.
AC Q8YNW7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Putative diflavin flavoprotein A 4;
DE EC=1.-.-.-;
GN Name=dfa4; OrderedLocusNames=all4444;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; 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; BAB76143.1; -; Genomic_DNA.
DR PIR; AD2361; AD2361.
DR RefSeq; WP_010998577.1; NZ_RSCN01000054.1.
DR AlphaFoldDB; Q8YNW7; -.
DR SMR; Q8YNW7; -.
DR STRING; 103690.gene:10496493; -.
DR KEGG; ana:all4444; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OrthoDB; 9807946at2; -.
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 CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR045761; ODP_dom.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR PANTHER; PTHR32145:SF32; DIFLAVIN FLAVOPROTEIN A 4-RELATED; 1.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF19583; ODP; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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..575
FT /note="Putative diflavin flavoprotein A 4"
FT /id="PRO_0000216796"
FT DOMAIN 263..405
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 41..234
FT /note="Zinc metallo-hydrolase"
FT REGION 429..575
FT /note="Flavodoxin-reductase-like"
SQ SEQUENCE 575 AA; 63749 MW; B94428B16882FB70 CRC64;
MTIATSSRPR DVQVADIGEH TLILRSRTWE RLKFEVEYSR QRGTTANSYL IQADKKALID
PPGESFTAIY LEQLAQYLDF TTLDYIILGH VNPNRRVTLQ ELLSKAPQAT LICSRPAANA
LKTAFPEWES RIQAVRFEDI LDLGQGHQLT FVTAPTPRWP DGLFTYDSAT KILYTDKFFG
AHICEDTLFD EDWKKLDAER HYYFDCLHAP QAKQVEAALD KVVMLGARSY APGHGPVVRY
SLSRFTYDYR QWCQGQKSQD LNVALLYTSA YGNTGILANA IAQGLVQNDV NVQSVNCELA
DTAEITRIVE ACDGIIIGSP TLGGHAPTQI QTALGIVLST AAKTKLAGVF GSYGWSGEAI
DLIESKLKDA NYRLGFDTIR VRFSPTPEIL QQCQAAGATF AQTLKKNKKL RTPRQVIPEA
KIDRTEQAVG RIIGSLCVVT TRDQESHKGI LTSWVSQATF NPPGIMMAIA QEQNADLMSH
TGDQFVLNIL KEGRNVRRYF SRQSTLGDNP FANLKTKTAD NGCLILTEAL AYLECTVTNQ
LECGDRLLIY AVVDKGEVLA NDGVTAVEHR KSGSH
//
