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Database: UniProt
Entry: A0A2S9BVL1_9MICO
LinkDB: A0A2S9BVL1_9MICO
Original site: A0A2S9BVL1_9MICO 
ID   A0A2S9BVL1_9MICO        Unreviewed;       303 AA.
AC   A0A2S9BVL1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PRB65695.1};
GN   ORFNames=CQ034_00090 {ECO:0000313|EMBL:PRB65695.1};
OS   Microbacterium sp. MYb45.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1827294 {ECO:0000313|EMBL:PRB65695.1, ECO:0000313|Proteomes:UP000238044};
RN   [1] {ECO:0000313|EMBL:PRB65695.1, ECO:0000313|Proteomes:UP000238044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb45 {ECO:0000313|EMBL:PRB65695.1,
RC   ECO:0000313|Proteomes:UP000238044};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) 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:PRB65695.1}.
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DR   EMBL; PCPG01000001; PRB65695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9BVL1; -.
DR   OrthoDB; 502624at2; -.
DR   Proteomes; UP000238044; 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   CDD; cd06185; PDR_like; 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; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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:ARBA00022723}.
FT   DOMAIN          1..93
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          218..303
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   303 AA;  32948 MW;  5C940E14C4162ECF CRC64;
     MRWEARDVLS LELDDPTGAP LPAWEPGAHI DLRFANGVER QYSLCSDPAD RTAWRVAILA
     ESPSRGGSRY VHQSLRVGEL VTVSAPINHF ALTPATEYVF VAGGIGITPI LPMLSEAVRR
     GIPWRLAYLG STEERMAFLR YPQLAGGETL LVRGDADERL DLAAWIGVPS AGTAVYACGP
     ERMLDALEQL SLDWPHGALH LERFQPKTFG ESQGADTFEV VATRSDLVVT VDRGCSILEM
     LESAGIGVPS SCLEGVCGTC ETTVIDGTPE HRDSILTPDE RESNETMMIC VSRSLGERLV
     LDI
//
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