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Database: UniProt
Entry: A0A0H2L157_9MICO
LinkDB: A0A0H2L157_9MICO
Original site: A0A0H2L157_9MICO 
ID   A0A0H2L157_9MICO        Unreviewed;       781 AA.
AC   A0A0H2L157;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KLN33917.1};
GN   ORFNames=FB00_14785 {ECO:0000313|EMBL:KLN33917.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN33917.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN33917.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN33917.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:KLN33917.1}.
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DR   EMBL; JNBQ01000023; KLN33917.1; -; Genomic_DNA.
DR   RefSeq; WP_047233639.1; NZ_JNBQ01000023.1.
DR   AlphaFoldDB; A0A0H2L157; -.
DR   STRING; 264251.FB00_14785; -.
DR   PATRIC; fig|264251.5.peg.3013; -.
DR   Proteomes; UP000035265; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF51; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT   DOMAIN          355..530
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          756..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  81692 MW;  08E53DEBC3D24AD8 CRC64;
     MTDYGHPLRF GTFVTPSAPD PEATVGLARL AEDLGYDLVT FQDHPYQPRL LDTWTLLSYV
     ASATERIHVA PDVVNVPMRQ PAVLARAAAS LDLLSDGRVD LALGAGAFWD AMVSMGVERL
     TPGESVDALA EAIEVIRAIW GEDGDGELFV PGRHHRLDGA TAGPGTTRRI PVWLGALGPR
     MLRLVGEKAD GWLPSLGRVG LDGLRAGNAR IDEAATAVGR DPREITRLLN VSGAFGTGDG
     GGGLGGAPDL AGPPEAWIER LLPLLLEEGV STLVLATDDE RTTCRFAEEV APVLRDAVAA
     GRASHGTDTS RVVPLAVRAA RRPGIAYDDV PASLAERAVE PGDAAYAGVR SNYLRGGSPG
     LVLRPRDTAE VVEALAFARG QQVTRTVPLS VRSGGHGISG RSTNDGGIVL DLGALDAVEV
     LDDAARLVRV GPGARWGEVA AALAPRGWAI TSGDYGGVGV GGLATAGGIG FLGRAHGLTI
     DHVRAVEVVL ADGSVVRASA EENPDLFWAV RGAGSQVGIV TSFELVADEV SAVGFAQMVH
     DASDLAGFLE RWGATVEASP RDTTSFLIVG RPRPGQPVVA QSMTMVDSDD PDTVLARLQP
     FAAISPLLAQ ATAQIVPYDA VVSAPAPGPH GGRGEPVSRS GLLEHLTPEA SARLAGLVAS
     GDTYFFQIRS TGGAASDVPA DATAYGHRSA NFSVVAMGAS RSRLDARWDA LADVFEGMYL
     SFDTDLRPER VADAFPPATL SRLREVKRRV DPTNVFRDNL PVLGPDPLDR EPREAAPAPA
     R
//
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