ID A0A2V1K7A1_9ACTO Unreviewed; 345 AA.
AC A0A2V1K7A1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PWF27326.1};
GN ORFNames=DD236_02770 {ECO:0000313|EMBL:PWF27326.1};
OS Ancrocorticia populi.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Ancrocorticia.
OX NCBI_TaxID=2175228 {ECO:0000313|EMBL:PWF27326.1, ECO:0000313|Proteomes:UP000245283};
RN [1] {ECO:0000313|Proteomes:UP000245283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sk1b4 {ECO:0000313|Proteomes:UP000245283};
RA Li Y.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:PWF27326.1}.
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DR EMBL; QETB01000001; PWF27326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1K7A1; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000245283; Unassembled WGS sequence.
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; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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; PS00197; 2FE2S_FER_1; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000245283}.
FT DOMAIN 5..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 105..209
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 36886 MW; EE5337F722A00C23 CRC64;
MSTSYTHSLT TSDGTHLTLQ GGPESSIIEA AEEAGMLLPS SCRAGNCGAC HAHAEGQYRL
GDHAKTVLDD EAEVAGDVLL CRTYPEGPLN IRLPYEQGRI ISGKIPERRA TVKMCEETAE
DTIHLALELG PGEDGALGCE FDPGQFLELT IPGTATRRSY SLANCPNWDG TAELFIKLRE
GGEFSEFLGG VSAGQEIDVR GPQGAFGIRD TGIRPRWFIA GGTGLSPLLS MLRHMADWGE
SHPAELWFGV QTEEEIFGTD VMEDIAASMP GFRYEVFVGE PTKGWTGAVG TPLDRLATEL
AESPAPPDIY VCGPPGMVSA TKKIVEQAGL PEERVIVESF APSSS
//
