ID Q5WI15_SHOC1 Unreviewed; 459 AA. AC Q5WI15; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 04-NOV-2026, entry version 109. 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 Name=sacA {ECO:0000313|EMBL:BAD63990.1}; GN OrderedLocusNames=ABC1455 {ECO:0000313|EMBL:BAD63990.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63990.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD63990.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63990.1, RC ECO:0000313|Proteomes:UP000001168}; RA Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.; RT "Molecular cloning and nucleotide sequence of the gene for an alkaline RT protease from the alkalophilic Bacillus sp. KSM-K16."; RL J. Ferment. Bioeng. 78:105-108(1994). RN [2] {ECO:0000313|EMBL:BAD63990.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63990.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=7632397; DOI=10.1007/s002530050437; RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., RA Kawai S., Ito S.; RT "Purification and properties of an alkaline protease from alkalophilic RT Bacillus sp. KSM-K16."; RL Appl. Microbiol. Biotechnol. 43:473-481(1995). RN [3] {ECO:0000313|EMBL:BAD63990.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63990.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=9278275; DOI=10.1093/protein/10.6.627; RA Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.; RT "High-resolution crystal structure of M-protease: phylogeny aided analysis RT of the high-alkaline adaptation mechanism."; RL Protein Eng. 10:627-634(1997). RN [4] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD63990.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63990.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=17429572; DOI=10.1007/s00792-007-0074-1; RA Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K., RA Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.; RT "Intragenomic diversity of the V1 regions of 16S rRNA genes in high- RT alkaline protease-producing Bacillus clausii spp."; RL Extremophiles 11:597-603(2007). 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|PROSITE-ProRule:PRU10067, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006627; BAD63990.1; -; Genomic_DNA. DR RefSeq; WP_011246299.1; NC_006582.1. DR AlphaFoldDB; Q5WI15; -. DR STRING; 66692.ABC1455; -. DR PaxDb; 66692-ABC1455; -. DR KEGG; bcl:ABC1455; -. DR eggNOG; COG1621; Bacteria. DR HOGENOM; CLU_001528_7_1_9; -. DR OMA; ADIPHGQ; -. DR OrthoDB; 9759709at2; -. DR UniPathway; UPA00238; -. DR Proteomes; UP000001168; 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 Gene3D; 2.60.120.560; Exo-inulinase, domain 1; 1. DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR051214; GH32_Enzymes. 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:UP000001168}. FT DOMAIN 12..315 FT /note="Glycosyl hydrolase family 32 N-terminal" FT /evidence="ECO:0000259|Pfam:PF00251" FT DOMAIN 338..439 FT /note="Glycosyl hydrolase family 32 C-terminal" FT /evidence="ECO:0000259|Pfam:PF08244" FT ACT_SITE 22 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10067" SQ SEQUENCE 459 AA; 53081 MW; B3B9CADB9B2F2355 CRC64; MSKSDAYNLK YHITPTHGLL NDPNGLAYFQ GQYHVFYQWN PYGTEHKNKS WGHVVSDDLV NWHRKETALV PSEWYDKDGI YSGGSIVHEG KLYLFYTGNV INKDGTRASY QCAAVSEDGH QFQKLGPLFE HPAGYTRHVR DPKVWKDDSG NWWLIVGAQR EDLTGDALVY KSEDLISWSC QGSFLEQEHS FGYMWECPDV LQFPEHDVFV FSPQGLPEEG DQYKNPNQSG YIIGRISESG KFLGTLSDFN ELDRGFDFYA PQTFKVNNRI LMFGWMSAMT EETEQAVPTI EEGWVHALTL PREIVFADGV LYQRPLHELQ LLRQHEVHEG ISNSGQWSLP SLAAEVVIRF MEQPDSFQLI IRNSVQIDYD HEQNSLTVWR TNWLTNEKEH RRAVLGHSLA ELHMFIESSS IELFVNEGEE VFSLRYFLED TNERSVRFES DCSEAVLSMY RLQESIDEE //