ID L8LSV3_9CHRO Unreviewed; 573 AA.
AC L8LSV3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative flavoprotein {ECO:0000313|EMBL:ELR99121.1};
GN ORFNames=GLO73106DRAFT_00029690 {ECO:0000313|EMBL:ELR99121.1};
OS Gloeocapsa sp. PCC 73106.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR99121.1, ECO:0000313|Proteomes:UP000011180};
RN [1] {ECO:0000313|EMBL:ELR99121.1, ECO:0000313|Proteomes:UP000011180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR99121.1,
RC ECO:0000313|Proteomes:UP000011180};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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.
CC {ECO:0000256|ARBA:ARBA00025633}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavodoxin
CC reductase family. {ECO:0000256|ARBA:ARBA00006098}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELR99121.1}.
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DR EMBL; ALVY01000153; ELR99121.1; -; Genomic_DNA.
DR RefSeq; WP_006528039.1; NZ_ALVY01000153.1.
DR AlphaFoldDB; L8LSV3; -.
DR STRING; 102232.GLO73106DRAFT_00029690; -.
DR PATRIC; fig|102232.3.peg.1062; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000011180; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022982};
KW Reference proteome {ECO:0000313|Proteomes:UP000011180};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 258..396
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 573 AA; 63000 MW; 1E71CA05C97671B0 CRC64;
MSKSRDVQVS YITEHTRVFR SRTWDRLKFE IEYGLEKGTT ANSFLIESDK TILINPPGES
FTEIFLQALQ DRIDPQSIDY LILSHVNLNR CTTIKSLLNI APQLTLICSN PGAITLQNTL
TDLPLNLKII KTEENLNIGQ GHDLEFIPTP IPRWPDELCI YDPKTQILYT DKLFGAHVCG
DQVLDEGWTI YQEDRRYYFD CVMAPSARQV ITALNKLSTK EAKIYATGHG PLVRYGLKEL
TRAYLEWSEN QQKQELSVAL IYASAYGNTA TLAQAIALGI TKAGVRVESL NAEIASPEDI
KTAVTQAEGF IFGSPTLGGH PPTQIQTALG ITLATASKNK LTGVFGSYGW SGEAIDILEG
KLRDGGYRFG IDTIRVKFKP TEVVLKSCEE AGTDFAQALK KQLKASKPKP SVNASLADRT
QQALGRVVGS LCVVTTVNGE VKGGMLASWV SQATFNPPGL TIAVAKERAI ESLLYSGSVF
VLNVLEQGKH LGLMKHFLKP FAPGEDRFEG VDMAIAPNGC PILQDALAYV ECTVSQRLEC
GDHWLIYAIA QTGKVFNTEG LTAVHHRQSG NHY
//
