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Database: UniProt
Entry: A0A0S9BT50_9MICC
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ID   A0A0S9BT50_9MICC        Unreviewed;       507 AA.
AC   A0A0S9BT50;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KQN84569.1};
GN   ORFNames=ASE96_17085 {ECO:0000313|EMBL:KQN84569.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN84569.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN84569.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN84569.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN84569.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN84569.1,
RC   ECO:0000313|Proteomes:UP000051467};
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   -!- 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:KQN84569.1}.
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DR   EMBL; LMLR01000016; KQN84569.1; -; Genomic_DNA.
DR   RefSeq; WP_056433859.1; NZ_LMLR01000016.1.
DR   AlphaFoldDB; A0A0S9BT50; -.
DR   STRING; 1736232.ASE96_17085; -.
DR   OrthoDB; 9767869at2; -.
DR   Proteomes; UP000051467; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   CDD; cd03477; Rieske_YhfW_C; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR038010; YhfW_C.
DR   PANTHER; PTHR13847:SF274; RIESKE 2FE-2S IRON-SULFUR PROTEIN YHFW-RELATED; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 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          415..496
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   507 AA;  52348 MW;  B92666A29C236C8C CRC64;
     MNEQPVGRLL SLWSATGGTA SYAPLEASLD VDVAVIGGGV AGLTAALALK RAGQTVAVLE
     AAGVGTGVTG NTTGKVTSLH RLAYSELAAR HGAGTAGTYG QANEAAIEHI AGVVLAEGID
     CGFRRVANYT YAESGRALAL VREEAALAAR LGLPASFTTD VPLPFAVRGA VRFDGQAQLH
     ALRYVQGLAR AVDGNGSFVF EESPATGFRD GSPAVVATER GSIRATEIIV ATNLPFGDHG
     LFAGRCYAHR SYLVAGRSAV PPLDATFVSV DEPMRSILTV DVGGSSYVLA GGEGHPATES
     VDSAERYRRL AAFARDRLGA GEIAFRWSTQ DAMPADGLPY VGLMAPEFRH VHVITGLRKW
     GLTNGTAAAL ILRDTLCGTD NPWAAVFDST RSAHATGAVP AVPKESVPDA DGAAPSEMAV
     PEVAPGEGKV VEVDGARTAV YVSPEGDVQA VSAVCTHLGC TVEFNSTDVT WDCPCHGSRF
     TTDGIVIQGP ATRNLAGPAP DRAESAR
//
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