ID I2HMW7_9BACI Unreviewed; 448 AA.
AC I2HMW7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EIF12076.1};
GN ORFNames=MY7_0370 {ECO:0000313|EMBL:EIF12076.1};
OS Bacillus sp. 5B6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF12076.1, ECO:0000313|Proteomes:UP000005799};
RN [1] {ECO:0000313|EMBL:EIF12076.1, ECO:0000313|Proteomes:UP000005799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5B6 {ECO:0000313|EMBL:EIF12076.1,
RC ECO:0000313|Proteomes:UP000005799};
RX PubMed=22740678; DOI=10.1128/JB.00682-12;
RA Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT Isolated from a Cherry Tree.";
RL J. Bacteriol. 194:3758-3759(2012).
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:EIF12076.1}.
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DR EMBL; AJST01000001; EIF12076.1; -; Genomic_DNA.
DR RefSeq; WP_007609656.1; NZ_AJST01000001.1.
DR AlphaFoldDB; I2HMW7; -.
DR PATRIC; fig|1127743.3.peg.353; -.
DR Proteomes; UP000005799; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 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; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 29..201
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 448 AA; 50108 MW; DD1447F284092974 CRC64;
MGSAQLTGRV IFKGDPGYTE AVKNWNPYVD VCPLVFVFAQ NSYDVSNAIK WAREKNVPMR
VRSGRHALDK NLSTVSDGIV IDVSDMNKVF LDEKNAVATV QTGIHVGPLV KGLAREGFMA
PFGDSPTVGI GGITMGGGFG VLSRSIGLIS DNLLALKMVD AKGRIIQANQ SRNEDLLWAS
RGGGGGNFGY NTQYTFKVHR APKTATVFNI IWPWEQLETV FKAWQKWAPF TDERLGCYLE
IYSKVNGLCH VEGLFLGSKP ELVQLLKPLL NAGTPAQTVI KTLYYPDCID FLDPDEPIPG
RSDQSVKFSS AWALNLWPEE PIAVMRQFLE KATGTETNFF FINWGGAISR VPSSETAFYW
RRPLFYTEWT ASWKNKSQEA SNLASVERVR QLMKPYVTGS YVNVPDQNIE NFGKAYYGSN
FARLQRIKAK YDPENVFRFP QSIPPSYK
//
