ID A0A0Q9KCI0_9MICO Unreviewed; 365 AA.
AC A0A0Q9KCI0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KRE39041.1};
GN ORFNames=ASG73_01365 {ECO:0000313|EMBL:KRE39041.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39041.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE39041.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39041.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE39041.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE39041.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE39041.1}.
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DR EMBL; LMRZ01000001; KRE39041.1; -; Genomic_DNA.
DR RefSeq; WP_055989703.1; NZ_LMRZ01000001.1.
DR AlphaFoldDB; A0A0Q9KCI0; -.
DR STRING; 1736393.ASG73_01365; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000051572; 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; 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; 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; 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; 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}.
FT DOMAIN 2..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 103..207
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 365 AA; 40384 MW; B74A3B9C9999E654 CRC64;
MTKYTITVEP VGREVQCDED QTILDACLRA GVWLPHSCTH GTCATCKVDK LDGEVDLGEA
STFALMDFER DEGKLLTCCA KPREDVTIEA DLDVDEDMEV FPVEDYTGTV VVLEDIAQDT
KRLVVELDRE IGFNAGQYMK FSVPVAEGDE AVDRTWSIGS PPGETTRLEF HIRNVPGGRG
TDGWVFKTLA KGDEVRMSGP YGRFVLKTGD DKHAILVGGG TGVAPLKSMV RHAFEAGEYE
GEITLYAGGR TRAHLYDVEA FRALEDEYDE FTYRPCLSDE TPEEVAADGD DPDGYAYGMV
TTVIEADHER LIGCRGYLCG PPPMVDAALK TLMSRRLFPR DIFREDFFDE SDKNGSGLKS
PLIKR
//
