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
//