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
//