ID J8HNS5_BACCE Unreviewed; 445 AA.
AC J8HNS5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=IIG_01988 {ECO:0000313|EMBL:EJR34742.1};
OS Bacillus cereus VD048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053226 {ECO:0000313|EMBL:EJR34742.1, ECO:0000313|Proteomes:UP000006960};
RN [1] {ECO:0000313|EMBL:EJR34742.1, ECO:0000313|Proteomes:UP000006960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD048 {ECO:0000313|EMBL:EJR34742.1,
RC ECO:0000313|Proteomes:UP000006960};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD048.";
RL Submitted (APR-2012) 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:EJR34742.1}.
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DR EMBL; AHEU01000010; EJR34742.1; -; Genomic_DNA.
DR RefSeq; WP_002013453.1; NZ_JH792310.1.
DR AlphaFoldDB; J8HNS5; -.
DR PATRIC; fig|1053226.3.peg.2016; -.
DR HOGENOM; CLU_018354_10_2_9; -.
DR Proteomes; UP000006960; 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 31..202
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 445 AA; 49375 MW; 818C3405EDFA0FC7 CRC64;
MSNQNIELTG RIVTPENPEY NSAREEFNTF FNKFPLIIVF AQNTQDVVNA VRWSRQYNVP
MRMRSGRHNY EGLSVNNAGI VIDVSEMKQL EIDHNGGTVT IGTGWRNLSL TETLAAEGLV
VPSGVCPTPG IAGVTLGGGH SILSRPWGLT LDHLIELEMV DANGCIVRAN AKHNSDLYWA
YRGAGGGNFG ICTSFKFRTH KINTVGFTEI SWDLTDLKSV LKSWQEYTLP CADKRLTSTL
FMSSEVEPSL LMQGVFLGSV QELQALLQPL LQAGSPLTVT IEEIPWVEAA TRIAATQPIE
PLPFKSVGPY VYALLPEEAL TIIEHFINNT PQHATTSVFF HGLGGAVAEI SNEATAYFYR
KALSNMSIFA TWNQAEGAAA SIRWTEDFRL AMLPFTKGVY VNTPDLSIKD WPDAYYSCNF
DRLMEVKAKY DPKNVFNFPQ SIPPF
//
