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Database: UniProt
Entry: A0A0Q9KBF1_9MICO
LinkDB: A0A0Q9KBF1_9MICO
Original site: A0A0Q9KBF1_9MICO 
ID   A0A0Q9KBF1_9MICO        Unreviewed;       951 AA.
AC   A0A0Q9KBF1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KRE38631.1};
GN   ORFNames=ASG73_05510 {ECO:0000313|EMBL:KRE38631.1};
OS   Janibacter sp. Soil728.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE38631.1, ECO:0000313|Proteomes:UP000051572};
RN   [1] {ECO:0000313|EMBL:KRE38631.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE38631.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE38631.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE38631.1,
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:KRE38631.1}.
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DR   EMBL; LMRZ01000003; KRE38631.1; -; Genomic_DNA.
DR   RefSeq; WP_055992749.1; NZ_LMRZ01000003.1.
DR   AlphaFoldDB; A0A0Q9KBF1; -.
DR   STRING; 1736393.ASG73_05510; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000051572; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          37..261
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          596..627
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   951 AA;  99941 MW;  8A733F43C061219B CRC64;
     MTSSPTLLTE ALHREGVTDA RTDALTIGMY ATDAGIYRVP PRAVVFPRHT DEIAATLSVA
     RELGIPITAR GAGTSCAGNA VGPGIVIDTA RYLGRVLEVD RESATALVEA GTVHATLQAR
     AREIGLRFGP DPSSHSRCTI GGMIGNNACG NRALGYGRTS DNVVGMDLLT AAGTHLTATT
     GVAGGLPSLT GDDALVARLT QLTDDHLDTV RTKFATFGRQ VSGYALEHLA PERGRDIGRM
     LVGSEGTLAV VTQARVRLVT DPPATSLVVL GFPDIYAAGD VAHLLKGLGA VAAEGIDSRI
     VDVVRTRRGP QAVPDLPRGA AWMLVEVPGE DAAAAHAAAE RVRREIEHTD SLVVTDPAHA
     RALWKIREDG AGLSARSPRD RPAHAGWEDA AVPPARLGDY LRAFDALLEE HDVQGLPYGH
     FGDGCLHIRL DIDLDAPDAT DRYRRFVEDA ADLVAAHGGS LSGEHGDGRA RSALLPRMYD
     AETMGLFGAV KRAFDPSNLL NPGILVDPAP VDADIRIPAA HKVTVPLAFG YPEDGGDFSQ
     AVHRCTGVGK CRAAGTSTTV MCPSYLATGE EKDSTRGRAR VLQEMLNGST ITGGWSAPEV
     HDALDLCLSC KGCSSDCPTG VDMATYKSEA LHQTYKGKLR PRSHYTLGRL PQMARLAARA
     PRLVNAMTSL PGLKKLTLPA AGVDPRRSIP SFARTTFRSW ATAEGMIASA AQAAGTDHPV
     ALFVDSFTDH FSPHVGRATV ALLREAGFTP FVPQEALCCG LTFISTGQLD AARSTLEDAA
     RALGPAVAAG IPVVGMEPSC TAALRHDLPR LVDSAVARQV AGGVRTVAEI LTSAIDEGRW
     TAPDLTGTEV VAQPHCHQHA VMSWSADEAL LARTGATVTR LGGCCGLAGN FGVELGHYEV
     SVKIAEQQLL PAMDAASPDA VVLADGFSCQ TQIADLSERA GVHLVELLAR T
//
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