ID M1ZH50_9FIRM Unreviewed; 366 AA.
AC M1ZH50;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:SHD75770.1};
GN ORFNames=CUESP1_0379 {ECO:0000313|EMBL:SHD75770.1};
OS [Clostridium] ultunense Esp.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC Schnuerera.
OX NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD75770.1, ECO:0000313|Proteomes:UP000245423};
RN [1] {ECO:0000313|EMBL:SHD75770.1, ECO:0000313|Proteomes:UP000245423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD75770.1};
RA Manzoor S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT669839; SHD75770.1; -; Genomic_DNA.
DR RefSeq; WP_005587952.1; NZ_LT669839.1.
DR AlphaFoldDB; M1ZH50; -.
DR HOGENOM; CLU_003827_7_2_9; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000245423; Chromosome chri.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000245423};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..125
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 128..234
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 366 AA; 41490 MW; 560FB96CEA4C66DF CRC64;
METILITTVT VTAFTGILAF LLTLADRTIA NYGEMKIVIN DDKEYIVDGG NTLLAALIDE
KIFIPSACGG KGTCGYCKVK ILEGGGPVLP TELPWLTEEE LKDKVRLSCQ CKIKEDMRIE
IPEELFNVRE YQVTVESIED MTPVIKKLRL RFKEGEEISF KPGQYIQLKA PIYEGNDEEV
YRAYSIASPP SEKSYIDLII GYVPGGIATT YVHKHLKVGD TVDINGPYGD FCYQDKYDNE
MILVAVGTGM APILSILYHM KDQDIKRKAR FYFGARTPED LFLLDELKEF EKALYDFEFI
PTLSRALDEH NWTGARGRVN VLLDEHIKNP DDKEAYLCGS PAMIDTVVEV LKEKGILEEH
IYYDKF
//
