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Database: UniProt
Entry: A0RAI8_BACAH
LinkDB: A0RAI8_BACAH
Original site: A0RAI8_BACAH 
ID   A0RAI8_BACAH            Unreviewed;       618 AA.
AC   A0RAI8;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Nucleotide sugar epimerase {ECO:0000313|EMBL:ABK84231.1};
GN   OrderedLocusNames=BALH_0862 {ECO:0000313|EMBL:ABK84231.1};
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK84231.1, ECO:0000313|Proteomes:UP000000761};
RN   [1] {ECO:0000313|EMBL:ABK84231.1, ECO:0000313|Proteomes:UP000000761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam {ECO:0000313|EMBL:ABK84231.1,
RC   ECO:0000313|Proteomes:UP000000761};
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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DR   EMBL; CP000485; ABK84231.1; -; Genomic_DNA.
DR   RefSeq; WP_001261164.1; NC_008600.1.
DR   AlphaFoldDB; A0RAI8; -.
DR   ESTHER; bachk-q6hgn4; 6_AlphaBeta_hydrolase.
DR   KEGG; btl:BALH_0862; -.
DR   HOGENOM; CLU_030014_0_0_9; -.
DR   OMA; QNGQHNH; -.
DR   Proteomes; UP000000761; Chromosome.
DR   CDD; cd05263; MupV_like_SDR_e; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48079:SF6; EPIMERASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48079; PROTEIN YEEZ; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
FT   DOMAIN          6..239
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          383..607
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   618 AA;  69323 MW;  D9F31D4F1CB19A90 CRC64;
     MRTVFLTGGT GFIGKQLVKE LAREDVKILL LVRAKSKATS IFQERGILKK EVMHFIEGDL
     TKIGLGLSAE DKERVLKTDV IIHAGGPMDI QATSNEAASV FLNGAKHISE LAKSIHQLKG
     LQQFIHVVGY MSPFDDKNSN IAIDVFKEGN NYLKIKNPYE RTKFLADLYI RHQASAIGYP
     LSVINPPTVV GSSKTGSTEQ IAGLGLLVMS MRRGLMPVIP GGKGYRLPLI SNDEFAKFIV
     QVFRLEQPTI QTYTLVEDKQ HDQNIAELLS IMSESMNMRA PKISVPMPLM KTIMNSGVSK
     ITKIPSDGLN FITKRKFSNV SAKKIMGEDW FKKTSVMKFL PAVVADLDYR MIYQNGQHNH
     LFKRTLCDNT TLYQLQGEGK PFILLHGLLS DGEDLFPLAQ ELHEKTGQPV WILDLPGLGR
     SPFKRDKNLL DIYLNVVKKL LEKATNGAHL IGHSFGAFIL LEALVQQYID KKYAITLLQP
     PVVKKNAKSL NVPQFMNKWT LKLATTNFIE RYLLSNGLFE SIESIPEHYI EKISKSFTSP
     RILNTTVQLN SLLLKNDQGD FNEVTKYNLH IIWGGYDRAY SAPSHVGKID FVPYGHHFPL
     SHPSETATLV IKNSNTSR
//
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