ID Q81HN0_BACCR Unreviewed; 491 AA.
AC Q81HN0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|ARBA:ARBA00019623, ECO:0000256|RuleBase:RU362110};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758, ECO:0000256|RuleBase:RU362110};
DE AltName: Full=Invertase {ECO:0000256|ARBA:ARBA00033367, ECO:0000256|RuleBase:RU365015};
GN OrderedLocusNames=BC_0774 {ECO:0000313|EMBL:AAP07765.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP07765.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP07765.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
CC -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC source. {ECO:0000256|RuleBase:RU365015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000256|RuleBase:RU362110};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|ARBA:ARBA00004914, ECO:0000256|RuleBase:RU365015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR EMBL; AE016877; AAP07765.1; -; Genomic_DNA.
DR RefSeq; NP_830564.1; NC_004722.1.
DR RefSeq; WP_000049747.1; NC_004722.1.
DR AlphaFoldDB; Q81HN0; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; bce:BC0774; -.
DR PATRIC; fig|226900.8.peg.717; -.
DR HOGENOM; CLU_001528_7_1_9; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd18623; GH32_ScrB-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT DOMAIN 32..333
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 336..476
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 491 AA; 57221 MW; 31D12F2C78EB484B CRC64;
MSKYKTILQS NKDELHSLYE IANQDSWKPI YHIHPPFGLM NDPNGVSYYN DEYHVFYQWY
PFGPIHGMKH WGHVRSKDLI NWERMPVAII PTESYESHGA YSGSAIVKDG LLHLLYTGNI
KKPDDSRDAK QCMASMDSQY TMTKYSNNPV IDIIPDGYTK HVRDPKVWKH NDMYYMLLGA
QRENKTGTLL LYKSQDLYNW HFQGEITTNL KEFGFMWECP DYFQLSGKDV LLFSPQGIEK
DGENFHNVYN VVYAIGHFDI KNLYFHVDSY YEADKGFDFY APQTLEDSTS RRLLFAWAGS
SEITYPSDDY MWAHCLTLPR ELTLEDNILK QKPVSELTKL RTTKKDISGD ITAGLNVLST
LDDEDSYELI VTLKTEDAKR FGLSLFHNEE ECFPITFNRE QGTISIDRGN FYHQFGGEYG
FERCKKIDIQ DTIELQIFVD KSIVEIFLYD GSTVFTSRVF PRKDMKHHIA IFSDAKLNFT
ITQYKLKRGI V
//
