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Database: UniProt
Entry: A0A1B1KZT1_BACTU
LinkDB: A0A1B1KZT1_BACTU
Original site: A0A1B1KZT1_BACTU 
ID   A0A1B1KZT1_BACTU        Unreviewed;       213 AA.
AC   A0A1B1KZT1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   08-OCT-2025, entry version 42.
DE   SubName: Full=Fuculose phosphate aldolase {ECO:0000313|EMBL:ARP55796.1};
GN   ORFNames=CAB88_01135 {ECO:0000313|EMBL:ARP55796.1};
OS   Bacillus thuringiensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1428 {ECO:0000313|EMBL:ARP55796.1, ECO:0000313|Proteomes:UP000194143};
RN   [1] {ECO:0000313|EMBL:ARP55796.1, ECO:0000313|Proteomes:UP000194143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10792 {ECO:0000313|EMBL:ARP55796.1,
RC   ECO:0000313|Proteomes:UP000194143};
RA   Oh D.-H., Park B.-J., Shuai W., Chelliah R.;
RT   "Complete Genome Sequence of Bacillus thuringiensis type Strain ATCC
RT   10792.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
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DR   EMBL; CP021061; ARP55796.1; -; Genomic_DNA.
DR   RefSeq; WP_000926554.1; NZ_VLJE01000077.1.
DR   SMR; A0A1B1KZT1; -.
DR   Proteomes; UP000194143; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.40.225.10:FF:000005; L-fuculose phosphate aldolase; 1.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   InterPro; IPR050197; Aldolase_class_II_sugar_metab.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   NCBIfam; NF005302; PRK06833.1; 1.
DR   PANTHER; PTHR22789:SF0; 3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194143}.
FT   DOMAIN          8..184
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   213 AA;  23669 MW;  9B59A967AFF2E6BC CRC64;
     MLLQKEREEI VAYGKKMISS GLTKGTGGNI SIFNREQGLV AISPSGLEYY ETKPEDVVIL
     NLDGEVVEGE RKPSSELDMH LIYYRKREDI NALVHTHSPY AKTIASLGWE LPAVSYLIAF
     AGPNVRCAPY ETFGTKQLAD AAFEGMIDRR AVLLANHGLI AGANNIKMAF TVAEEIEFCA
     QIYYQTKSIG EPKLLPEDEM ENLAKKFEGY GQQ
//
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