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Database: UniProt
Entry: A1BYK0_BACCE
LinkDB: A1BYK0_BACCE
Original site: A1BYK0_BACCE 
ID   A1BYK0_BACCE            Unreviewed;       282 AA.
AC   A1BYK0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=ThiF family protein {ECO:0000313|EMBL:ABK00540.1};
GN   ORFNames=BcAH187_pCER270_0059 {ECO:0000313|EMBL:ABK00540.1},
GN   pPER272_0031 {ECO:0000313|EMBL:ABK01164.1}, pPER272_AH820_0031
GN   {ECO:0000313|EMBL:ABK00899.1};
OS   Bacillus cereus.
OG   Plasmid pCER270 {ECO:0000313|EMBL:ABK00540.1}, and
OG   Plasmid pPER272 {ECO:0000313|EMBL:ABK00899.1}.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396 {ECO:0000313|EMBL:ABK00540.1};
RN   [1] {ECO:0000313|EMBL:ABK00540.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AH187 {ECO:0000313|EMBL:ABK00540.1}, AH818
RC   {ECO:0000313|EMBL:ABK01164.1}, and AH820
RC   {ECO:0000313|EMBL:ABK00899.1};
RC   PLASMID=pCER270 {ECO:0000313|EMBL:ABK00540.1}, and pPER272
RC   {ECO:0000313|EMBL:ABK00899.1};
RX   PubMed=17041058; DOI=10.1128/JB.01313-06;
RA   Rasko D.A., Rosovitz M.J., Okstad O.A., Fouts D.E., Jiang L., Cer R.Z.,
RA   Kolsto A.B., Gill S.R., Ravel J.;
RT   "Complete sequence analysis of novel plasmids from emetic and periodontal
RT   Bacillus cereus isolates reveals a common evolutionary history among the B.
RT   cereus-group plasmids, including Bacillus anthracis pXO1.";
RL   J. Bacteriol. 189:52-64(2007).
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DR   EMBL; DQ889676; ABK00540.1; -; Genomic_DNA.
DR   EMBL; DQ889677; ABK00899.1; -; Genomic_DNA.
DR   EMBL; DQ889678; ABK01164.1; -; Genomic_DNA.
DR   RefSeq; WP_000029264.1; NZ_MQTC01000007.1.
DR   RefSeq; YP_001967202.1; NC_010924.1.
DR   PATRIC; fig|1396.421.peg.604; -.
DR   OMA; NGSHFFR; -.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd01483; E1_enzyme_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:ABK00540.1}.
FT   DOMAIN          16..144
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   282 AA;  31479 MW;  2233142871E46AB3 CRC64;
     MSIVIDIAEG KKIVPHIVLV GAGGNGGLIL QHIAQMMSIF QLDGEIVVAD PDTVEEKNLG
     NQLFIRPDVG KYKAEVLARR YKAGYNVPIS SFTSQYIEDI ETMQQLFGNK YDLLKKQHKD
     DYLYLPIVIG AVDNMFSREV FHQFFHQSDN LLYIDVGNTA VTVPDNWREV NKRHWTPQQI
     ADYKNSGYNG QAVCGVKLNG EVILSPLGDL FPDAFTKKET APSQLSCSEL AASEPQRVIT
     NKFAAMTVAQ FVNELFDEGT VSNHYIIFQA QKAFMKAAPI EG
//
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