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Database: UniProt
Entry: A0A196S3L2_BLAHN
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Original site: A0A196S3L2_BLAHN 
ID   A0A196S3L2_BLAHN        Unreviewed;       758 AA.
AC   A0A196S3L2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Hydrogenase {ECO:0000313|EMBL:OAO11745.1, ECO:0000313|EMBL:OAO16785.1};
GN   ORFNames=AV274_1483 {ECO:0000313|EMBL:OAO16785.1}, AV274_6580
GN   {ECO:0000313|EMBL:OAO11745.1};
OS   Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO11745.1, ECO:0000313|Proteomes:UP000078348};
RN   [1] {ECO:0000313|EMBL:OAO11745.1, ECO:0000313|Proteomes:UP000078348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348}, and
RC   NandII {ECO:0000313|EMBL:OAO11745.1};
RA   Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA   Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA   Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA   Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT   "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NARF family.
CC       {ECO:0000256|ARBA:ARBA00006596}.
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:OAO11745.1}.
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DR   EMBL; LXWW01000580; OAO11745.1; -; Genomic_DNA.
DR   EMBL; LXWW01000060; OAO16785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A196S3L2; -.
DR   STRING; 478820.A0A196S3L2; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000078348; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.1780; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009016; Fe_hydrogenase.
DR   InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR   InterPro; IPR003149; Fe_hydrogenase_ssu.
DR   InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR   InterPro; IPR013352; Fe_hydrogenase_subset.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   NCBIfam; TIGR02512; FeFe_hydrog_A; 1.
DR   PANTHER; PTHR11615:SF6; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR   Pfam; PF02906; Fe_hyd_lg_C; 1.
DR   Pfam; PF02256; Fe_hyd_SSU; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   SMART; SM00902; Fe_hyd_SSU; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023014};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078348}.
FT   DOMAIN          30..109
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          148..178
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          191..220
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          610..754
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   REGION          584..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  83340 MW;  80BF99B0EF99C033 CRC64;
     MLSRLSRIAT TKSMLVMNAA RSFAAEAQGK LVSVKINGNE YKVPEGMTVL EACQAQGIHV
     PFVCHHPRLK PLGKCRVCVV EIRGDEFPIK TSCNTKVEEG MDIWTNSPKA RSASNEALKT
     LMAGTPIDTK FKTMEMDEVL TESADDCYAL HRDMSRCVDC KRCARACSEL QGMNVLENNP
     QEGGFPVVPT GYHLLKDTEC ISCGQCNVVC PTGAIVEQSH IPRVKQAMKA GKVMVMQTAP
     ATRVAFGENF GREPGEITTG KMIACAKALG FQYVFDTNFG ADMTIMEEGT ELLERIKNNG
     PFPMFTSCCP GWVNMAEKCY PEILPNLSSC RSPHMMVGST LKTYWAKKMN LKPEDIYVVS
     LMPCTAKKDE IERKNMWLDE KTPFVDAVLT TKELGDFCKQ EGITNWDNMA EMPFDTPLGT
     SSGAGDIFGV SGGVMEAALR TAYQLQTGKP LEKIVVDEAR GLDGTKRFSV DMNGKKINCA
     VVHSKFAREL VENVKAGKED LQFVEVMACP GGCISGGGQP HSNRADTIEK RMNAIYKIDA
     GKTLRRSMDN PEIQTLYKEF FEKPNSHKAH ELLHTTYAPQ YVRSREEKVE EPAEAGGEGG
     EGSDVGEDGV TILYGSETGT TAKAAKALQS KFKAAGISSA VIPMNKIDVE SLPEKKKLVL
     MTCTYGAGEF PAMAQEFWEN LSDESLDDDF LEGVEFGVFG LGSKAFKQFC EAAHQLDERM
     EELGAERVVD CGEGNEKDPQ QYKTAFEPWS KEAVEAFK
//
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